(data stored in ACNUC7421 zone)

SWISSPROT: KAD_BACSU

ID   KAD_BACSU               Reviewed;         217 AA.
AC   P16304;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 2.
DT   11-DEC-2019, entry version 165.
DE   RecName: Full=Adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
DE            Short=AK {ECO:0000255|HAMAP-Rule:MF_00235};
DE            EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00235};
DE   AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00235};
DE   AltName: Full=ATP:AMP phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00235};
DE   AltName: Full=Adenylate monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_00235};
DE   AltName: Full=Superoxide-inducible protein 16;
DE            Short=SOI16;
GN   Name=adk {ECO:0000255|HAMAP-Rule:MF_00235}; OrderedLocusNames=BSU01370;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2113521; DOI=10.1093/oxfordjournals.jbchem.a123093;
RA   Nakamura K., Nakamura A., Takamatsu H., Yoshikawa H., Yamane K.;
RT   "Cloning and characterization of a Bacillus subtilis gene homologous to E.
RT   coli secY.";
RL   J. Biochem. 107:603-607(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC   3610 / VKM B-501;
RX   PubMed=8635744; DOI=10.1016/0378-1119(95)00757-1;
RA   Suh J.-W., Boylan S.A., Oh S.H., Price C.W.;
RT   "Genetic and transcriptional organization of the Bacillus subtilis spc-
RT   alpha region.";
RL   Gene 169:17-23(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RX   PubMed=2139212; DOI=10.1093/nar/18.6.1647;
RA   Yoshikawa H., Doi R.H.;
RT   "Sequence of the Bacillus subtilis spectinomycin resistance gene region.";
RL   Nucleic Acids Res. 18:1647-1647(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
RC   STRAIN=168;
RX   PubMed=2110998; DOI=10.1111/j.1365-2958.1990.tb00597.x;
RA   Suh J.-W., Boylan S.A., Thomas S.M., Dolan K.M., Oliver D.B., Price C.W.;
RT   "Isolation of a secY homologue from Bacillus subtilis: evidence for a
RT   common protein export pathway in eubacteria.";
RL   Mol. Microbiol. 4:305-314(1990).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-20.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [7]
RP   ZINC ION.
RX   PubMed=1554691; DOI=10.1021/bi00127a002;
RA   Glaser P., Presecan E., Delepierre M., Surewicz W.K., Mantsch H.H.,
RA   Barzu O., Gilles A.M.;
RT   "Zinc, a novel structural element found in the family of bacterial
RT   adenylate kinases.";
RL   Biochemistry 31:3038-3043(1992).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH BI-SUBSTRATE ANALOG
RP   AP5A AND ZINC, AND TEMPERATURE DEPENDENCE.
RX   PubMed=15100224; DOI=10.1074/jbc.m401865200;
RA   Bae E., Phillips G.N. Jr.;
RT   "Structures and analysis of highly homologous psychrophilic, mesophilic,
RT   and thermophilic adenylate kinases.";
RL   J. Biol. Chem. 279:28202-28208(2004).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1-216 IN COMPLEX WITH
RP   BI-SUBSTRATE ANALOG AP5A AND ZINC.
RX   PubMed=16713575; DOI=10.1016/j.molcel.2006.04.012;
RA   Counago R., Chen S., Shamoo Y.;
RT   "In vivo molecular evolution reveals biophysical origins of organismal
RT   fitness.";
RL   Mol. Cell 22:441-449(2006).
CC   -!- FUNCTION: Catalyzes the reversible transfer of the terminal phosphate
CC       group between ATP and AMP. Plays an important role in cellular energy
CC       homeostasis and in adenine nucleotide metabolism. {ECO:0000255|HAMAP-
CC       Rule:MF_00235}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00235};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is 45 degrees Celsius. Thermal denaturation
CC         midpoint (Tm) is 47.6 degrees Celsius and is raised to 66.0 degrees
CC         Celsius when AK is complexed with the inhibitor Ap5A.
CC         {ECO:0000269|PubMed:15100224};
CC   -!- PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP
CC       from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}.
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00235,
CC       ECO:0000269|PubMed:16713575}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- INDUCTION: By superoxide.
CC   -!- DOMAIN: Consists of three domains, a large central CORE domain and two
CC       small peripheral domains, NMPbind and LID, which undergo movements
CC       during catalysis. The LID domain closes over the site of phosphoryl
CC       transfer upon ATP binding. Assembling and dissambling the active center
CC       during each catalytic cycle provides an effective means to prevent ATP
CC       hydrolysis. Some bacteria have evolved a zinc-coordinating structure
CC       that stabilizes the LID domain. {ECO:0000255|HAMAP-Rule:MF_00235,
CC       ECO:0000305|PubMed:15100224, ECO:0000305|PubMed:1554691,
CC       ECO:0000305|PubMed:16713575}.
CC   -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00235}.
DR   EMBL; D00619; BAA00496.1; -; Genomic_DNA.
DR   EMBL; L47971; AAB06820.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11913.1; -; Genomic_DNA.
DR   EMBL; M31102; AAB59119.1; -; Genomic_DNA.
DR   EMBL; X51329; CAA35713.1; -; Genomic_DNA.
DR   PIR; JS0492; JS0492.
DR   RefSeq; NP_388018.1; NC_000964.3.
DR   RefSeq; WP_004399686.1; NZ_JNCM01000029.1.
DR   PDB; 1P3J; X-ray; 1.90 A; A=1-217.
DR   PDB; 2EU8; X-ray; 1.80 A; A/B=1-216.
DR   PDB; 2OO7; X-ray; 1.80 A; A/B=1-217.
DR   PDB; 2ORI; X-ray; 1.80 A; A/B=1-216.
DR   PDB; 2OSB; X-ray; 1.80 A; A/B=1-216.
DR   PDB; 2P3S; X-ray; 1.80 A; A=1-217.
DR   PDB; 2QAJ; X-ray; 1.80 A; A/B=1-217.
DR   PDB; 3DKV; X-ray; 1.82 A; A=1-217.
DR   PDB; 3DL0; X-ray; 1.58 A; A/B=1-216.
DR   PDB; 4MKF; X-ray; 1.70 A; A/B=1-217.
DR   PDB; 4MKG; X-ray; 1.45 A; A=1-217.
DR   PDB; 4MKH; X-ray; 1.50 A; A=1-212.
DR   PDB; 4QBF; X-ray; 1.80 A; A=1-217.
DR   PDB; 4QBG; X-ray; 1.37 A; B=1-217.
DR   PDB; 4TYP; X-ray; 2.90 A; A/B/C/D=1-217.
DR   PDB; 4TYQ; X-ray; 1.65 A; A/B=1-217.
DR   PDB; 5X6I; X-ray; 2.00 A; A=1-217.
DR   PDBsum; 1P3J; -.
DR   PDBsum; 2EU8; -.
DR   PDBsum; 2OO7; -.
DR   PDBsum; 2ORI; -.
DR   PDBsum; 2OSB; -.
DR   PDBsum; 2P3S; -.
DR   PDBsum; 2QAJ; -.
DR   PDBsum; 3DKV; -.
DR   PDBsum; 3DL0; -.
DR   PDBsum; 4MKF; -.
DR   PDBsum; 4MKG; -.
DR   PDBsum; 4MKH; -.
DR   PDBsum; 4QBF; -.
DR   PDBsum; 4QBG; -.
DR   PDBsum; 4TYP; -.
DR   PDBsum; 4TYQ; -.
DR   PDBsum; 5X6I; -.
DR   SMR; P16304; -.
DR   IntAct; P16304; 1.
DR   MINT; P16304; -.
DR   STRING; 224308.BSU01370; -.
DR   DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate.
DR   jPOST; P16304; -.
DR   PaxDb; P16304; -.
DR   PRIDE; P16304; -.
DR   EnsemblBacteria; CAB11913; CAB11913; BSU01370.
DR   GeneID; 938508; -.
DR   KEGG; bsu:BSU01370; -.
DR   PATRIC; fig|224308.179.peg.140; -.
DR   eggNOG; COG0563; LUCA.
DR   HOGENOM; HOG000238772; -.
DR   InParanoid; P16304; -.
DR   KO; K00939; -.
DR   OMA; FHNRMRV; -.
DR   PhylomeDB; P16304; -.
DR   BioCyc; BSUB:BSU01370-MONOMER; -.
DR   BRENDA; 2.7.4.3; 658.
DR   SABIO-RK; P16304; -.
DR   UniPathway; UPA00588; UER00649.
DR   EvolutionaryTrace; P16304; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044209; P:AMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd01428; ADK; 1.
DR   HAMAP; MF_00235; Adenylate_kinase_Adk; 1.
DR   InterPro; IPR006259; Adenyl_kin_sub.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR033690; Adenylat_kinase_CS.
DR   InterPro; IPR007862; Adenylate_kinase_lid-dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; PTHR23359; 1.
DR   Pfam; PF05191; ADK_lid; 1.
DR   PRINTS; PR00094; ADENYLTKNASE.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01351; adk; 1.
DR   PROSITE; PS00113; ADENYLATE_KINASE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P16304.
DR   SWISS-2DPAGE; P16304.
KW   3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Metal-binding; Nucleotide biosynthesis; Nucleotide-binding;
KW   Reference proteome; Transferase; Zinc.
FT   CHAIN           1..217
FT                   /note="Adenylate kinase"
FT                   /id="PRO_0000158730"
FT   NP_BIND         10..15
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   NP_BIND         57..59
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   NP_BIND         85..88
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   NP_BIND         136..137
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   REGION          30..59
FT                   /note="NMPbind"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   REGION          126..163
FT                   /note="LID"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   METAL           130
FT                   /note="Zinc; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   METAL           133
FT                   /note="Zinc; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   METAL           150
FT                   /note="Zinc; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   METAL           153
FT                   /note="Zinc; structural"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   BINDING         31
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   BINDING         36
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   BINDING         92
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   BINDING         127
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   BINDING         160
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   BINDING         171
FT                   /note="AMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   BINDING         199
FT                   /note="ATP; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00235,
FT                   ECO:0000269|PubMed:15100224, ECO:0000269|PubMed:16713575"
FT   STRAND          2..6
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           13..24
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   STRAND          28..30
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           31..41
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           44..53
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   TURN            54..56
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           61..72
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           75..77
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   STRAND          81..85
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           90..102
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   STRAND          109..114
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           117..124
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   STRAND          127..130
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   TURN            131..133
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   STRAND          136..138
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   TURN            139..141
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   TURN            151..153
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   STRAND          156..158
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           161..163
FT                   /evidence="ECO:0000244|PDB:4MKG"
FT   HELIX           165..188
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   STRAND          192..196
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           201..212
FT                   /evidence="ECO:0000244|PDB:4QBG"
FT   HELIX           213..215
FT                   /evidence="ECO:0000244|PDB:3DL0"
SQ   SEQUENCE   217 AA;  24119 MW;  ECB9ECF4F26A1E90 CRC64;
     MNLVLMGLPG AGKGTQGERI VEDYGIPHIS TGDMFRAAMK EETPLGLEAK SYIDKGELVP
     DEVTIGIVKE RLGKDDCERG FLLDGFPRTV AQAEALEEIL EEYGKPIDYV INIEVDKDVL
     MERLTGRRIC SVCGTTYHLV FNPPKTPGIC DKDGGELYQR ADDNEETVSK RLEVNMKQTQ
     PLLDFYSEKG YLANVNGQQD IQDVYADVKD LLGGLKK
//

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