(data stored in ACNUC7421 zone)

SWISSPROT: PKN1_BACSU

ID   PKN1_BACSU              Reviewed;         338 AA.
AC   P37562; O31415;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   11-DEC-2019, entry version 126.
DE   RecName: Full=Probable serine/threonine-protein kinase YabT;
DE            EC=2.7.11.1;
GN   Name=yabT; OrderedLocusNames=BSU00660;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.1;
CC   -!- INTERACTION:
CC       O34507:prkC; NbExp=2; IntAct=EBI-9303331, EBI-6667154;
CC       P45870:racA; NbExp=3; IntAct=EBI-9303331, EBI-5242400;
CC       P16971:recA; NbExp=2; IntAct=EBI-9303331, EBI-1535844;
CC       O31435:ybdM; NbExp=2; IntAct=EBI-9303331, EBI-5255200;
CC       P96716:ywqD; NbExp=3; IntAct=EBI-9303331, EBI-9302929;
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA05301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; D26185; BAA05301.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB11842.2; -; Genomic_DNA.
DR   PIR; S66096; S66096.
DR   RefSeq; NP_387947.2; NC_000964.3.
DR   RefSeq; WP_009966278.1; NZ_JNCM01000028.1.
DR   PDB; 6G4J; X-ray; 1.60 A; A=1-315.
DR   PDBsum; 6G4J; -.
DR   SMR; P37562; -.
DR   IntAct; P37562; 40.
DR   STRING; 224308.BSU00660; -.
DR   PaxDb; P37562; -.
DR   PRIDE; P37562; -.
DR   EnsemblBacteria; CAB11842; CAB11842; BSU00660.
DR   GeneID; 936964; -.
DR   KEGG; bsu:BSU00660; -.
DR   PATRIC; fig|224308.179.peg.66; -.
DR   eggNOG; COG0515; LUCA.
DR   HOGENOM; HOG000261702; -.
DR   InParanoid; P37562; -.
DR   KO; K08884; -.
DR   OMA; FYDRGYW; -.
DR   BioCyc; BSUB:BSU00660-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37562.
DR   SWISS-2DPAGE; P37562.
KW   3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..338
FT                   /note="Probable serine/threonine-protein kinase YabT"
FT                   /id="PRO_0000171182"
FT   DOMAIN          28..286
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   NP_BIND         34..42
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   ACT_SITE        148
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         55
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   HELIX           4..12
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          18..20
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   TURN            22..24
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          27..37
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          40..47
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          50..58
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           60..74
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          76..78
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          85..93
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   TURN            94..97
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          98..105
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           113..120
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           124..141
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           151..153
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          154..157
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   TURN            158..161
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   STRAND          162..166
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           183..185
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   TURN            187..191
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           199..215
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           225..234
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           237..241
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           243..251
FT                   /evidence="ECO:0000244|PDB:6G4J"
FT   HELIX           257..272
FT                   /evidence="ECO:0000244|PDB:6G4J"
SQ   SEQUENCE   338 AA;  37666 MW;  71896CE0A0A03470 CRC64;
     MMNDALTSLA CSLKPGTTIK GKWNGNTYTL RKQLGKGANG IVYLAETSDG HVALKVSDDS
     LSITSEVNVL KSFSKAQSVT MGPSFFDTDD AYIPSANTKV SFYAMEYIKG PLLLKYVSDK
     GAEWIPVLMI QLLSSLSVLH QQGWIFGDLK PDNLIVTGPP ARIRCIDVGG TTKEGRAIKE
     YTEFYDRGYW GYGTRKAEPS YDLFAVAMIM INSVHKKEFK KTNQPKEQLR SLIEGNPLLQ
     KYKKALFSAL NGDYQSADEM KKDMLDAGQK AAQRKQPIKA SPQPATRQRQ QKPRQGKITK
     TRYTPKQKPA KSGGLFETTL IVISVLALYF AYIIFFLI
//

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