(data stored in ACNUC7421 zone)

SWISSPROT: PXPB_BACSU

ID   PXPB_BACSU              Reviewed;         240 AA.
AC   P60495; P42967;
DT   01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 1.
DT   11-DEC-2019, entry version 104.
DE   RecName: Full=5-oxoprolinase subunit B {ECO:0000305};
DE            Short=5-OPase subunit B {ECO:0000305};
DE            EC=3.5.2.9 {ECO:0000269|PubMed:28830929};
DE   AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit B {ECO:0000305};
DE   AltName: Full=Antikinase KipI {ECO:0000303|PubMed:18823995};
DE   AltName: Full=Kinase A inhibitor;
DE   AltName: Full=Sporulation inhibitor KipI;
GN   Name=pxpB {ECO:0000303|PubMed:28830929};
GN   Synonyms=kipI {ECO:0000303|PubMed:9334321}, ycsJ;
GN   OrderedLocusNames=BSU04080;
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=8574415; DOI=10.1099/13500872-141-12-3241;
RA   Akagawa E., Kurita K., Sugawara T., Nakamura K., Kasahara Y., Ogasawara N.,
RA   Yamane K.;
RT   "Determination of a 17,484 bp nucleotide sequence around the 39 degrees
RT   region of the Bacillus subtilis chromosome and similarity analysis of the
RT   products of putative ORFs.";
RL   Microbiology 141:3241-3245(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(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   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT   the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [5]
RP   FUNCTION, PROBABLE INTERACTION WITH PXPC, INDUCTION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=168 / JH642;
RX   PubMed=9334321; DOI=10.1101/gad.11.19.2569;
RA   Wang L., Grau R., Perego M., Hoch J.A.;
RT   "A novel histidine kinase inhibitor regulating development in Bacillus
RT   subtilis.";
RL   Genes Dev. 11:2569-2579(1997).
RN   [6]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX   PubMed=28830929; DOI=10.1074/jbc.m117.805028;
RA   Niehaus T.D., Elbadawi-Sidhu M., de Crecy-Lagard V., Fiehn O., Hanson A.D.;
RT   "Discovery of a widespread prokaryotic 5-oxoprolinase that was hiding in
RT   plain sight.";
RL   J. Biol. Chem. 292:16360-16367(2017).
RN   [7] {ECO:0000244|PDB:2ZP2}
RP   X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 100-240, AND INTERACTION WITH
RP   KINA.
RX   PubMed=18823995; DOI=10.1016/j.jmb.2008.09.017;
RA   Jacques D.A., Langley D.B., Jeffries C.M., Cunningham K.A.,
RA   Burkholder W.F., Guss J.M., Trewhella J.;
RT   "Histidine kinase regulation by a cyclophilin-like inhibitor.";
RL   J. Mol. Biol. 384:422-435(2008).
RN   [8] {ECO:0000244|PDB:2KWA}
RP   STRUCTURE BY NMR OF 1-99, AND INTERACTION WITH PXPC.
RX   PubMed=21050859; DOI=10.1016/j.jmb.2010.10.047;
RA   Jacques D.A., Langley D.B., Hynson R.M., Whitten A.E., Kwan A., Guss J.M.,
RA   Trewhella J.;
RT   "A novel structure of an antikinase and its inhibitor.";
RL   J. Mol. Biol. 405:214-226(2011).
CC   -!- FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-glutamate
CC       coupled to the hydrolysis of ATP to ADP and inorganic phosphate
CC       (PubMed:28830929). In addition, is a potent inhibitor of the
CC       autophosphorylation reaction of kinase A (kinA) and its reverse
CC       reaction, but does not inhibit phosphate transfer to the Spo0F response
CC       regulator once kinase A is phosphorylated. Is an inhibitor of the
CC       catalytic domain of kinase A affecting the ATP/ADP reactions and not
CC       the phosphotransferase functions of this domain. The inhibition is non-
CC       competitive with respect to ATP (PubMed:9334321).
CC       {ECO:0000269|PubMed:28830929, ECO:0000269|PubMed:9334321}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC         phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC         Evidence={ECO:0000269|PubMed:28830929};
CC   -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC
CC       (PubMed:28830929). Interacts with PxpC (KipA) (PubMed:9334321,
CC       PubMed:21050859, PubMed:28830929). Interaction with PxpC prevents the
CC       inhibitory action of PxpB (KipI) (PubMed:9334321, PubMed:21050859).
CC       Interacts with KinA. Two PxpB monomers bind via their C-domains at a
CC       conserved proline in the KinA dimerization and histidine-
CC       phosphotransfer (DHp) domain (PubMed:18823995).
CC       {ECO:0000269|PubMed:18823995, ECO:0000269|PubMed:21050859,
CC       ECO:0000269|PubMed:28830929, ECO:0000269|PubMed:9334321}.
CC   -!- INDUCTION: Induced by glucose when readily available sources of
CC       nitrogen, such as ammonia or glutamine, are scarce. Transcriptionally
CC       activated by TnrA and repressed by KipR. {ECO:0000269|PubMed:9334321}.
CC   -!- DISRUPTION PHENOTYPE: Deletion of the gene enhances sporulation
CC       (PubMed:9334321). Deletion mutant grows less well than wild type on
CC       minimal medium with ammonium as nitrogen source and cannot grow on 5-
CC       oxoproline. Mutant lacks 5-oxoprolinase activity and accumulates 5-oxo-
CC       L-proline (PubMed:28830929). {ECO:0000269|PubMed:28830929,
CC       ECO:0000269|PubMed:9334321}.
CC   -!- SIMILARITY: Belongs to the PxpB family. {ECO:0000305}.
CC   -!- CAUTION: Was originally (PubMed:8574415 and PubMed:8969502) thought to
CC       be a longer ORF that encodes what is now known to be pxpB (kipI) and
CC       pxpC (kipA). {ECO:0000305|PubMed:9334321}.
DR   EMBL; D38161; BAA07361.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; D50453; BAA09039.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL009126; CAB12216.2; -; Genomic_DNA.
DR   PIR; G69765; G69765.
DR   RefSeq; NP_388290.2; NC_000964.3.
DR   RefSeq; WP_003234420.1; NZ_JNCM01000031.1.
DR   PDB; 2KWA; NMR; -; A=1-99.
DR   PDB; 2ZP2; X-ray; 3.01 A; A/B=100-240.
DR   PDBsum; 2KWA; -.
DR   PDBsum; 2ZP2; -.
DR   SMR; P60495; -.
DR   STRING; 224308.BSU04080; -.
DR   PaxDb; P60495; -.
DR   PRIDE; P60495; -.
DR   EnsemblBacteria; CAB12216; CAB12216; BSU04080.
DR   GeneID; 938256; -.
DR   KEGG; bsu:BSU04080; -.
DR   PATRIC; fig|224308.179.peg.434; -.
DR   eggNOG; ENOG4105P4J; Bacteria.
DR   eggNOG; COG2049; LUCA.
DR   HOGENOM; HOG000265713; -.
DR   InParanoid; P60495; -.
DR   KO; K06351; -.
DR   OMA; PYLGGMS; -.
DR   PhylomeDB; P60495; -.
DR   BioCyc; BSUB:BSU04080-MONOMER; -.
DR   EvolutionaryTrace; P60495; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.100.10; -; 1.
DR   InterPro; IPR003833; CT_C_D.
DR   InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR   InterPro; IPR010016; KipI_fam.
DR   PANTHER; PTHR34698; PTHR34698; 1.
DR   Pfam; PF02682; CT_C_D; 1.
DR   SMART; SM00796; AHS1; 1.
DR   SUPFAM; SSF50891; SSF50891; 1.
DR   TIGRFAMs; TIGR00370; TIGR00370; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P60495.
DR   SWISS-2DPAGE; P60495.
KW   3D-structure; ATP-binding; Hydrolase; Nucleotide-binding;
KW   Protein kinase inhibitor; Reference proteome; Sporulation.
FT   CHAIN           1..240
FT                   /note="5-oxoprolinase subunit B"
FT                   /id="PRO_0000084308"
FT   NP_BIND         194..201
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   STRAND          6..9
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   STRAND          11..18
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   HELIX           25..40
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   STRAND          46..51
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   STRAND          53..60
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   HELIX           62..66
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   HELIX           76..88
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   HELIX           89..91
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   HELIX           93..95
FT                   /evidence="ECO:0000244|PDB:2KWA"
FT   STRAND          101..109
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   TURN            110..112
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   HELIX           116..122
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   HELIX           127..134
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   STRAND          139..142
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   STRAND          152..154
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   HELIX           158..160
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   STRAND          176..181
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   STRAND          183..186
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   STRAND          196..200
FT                   /evidence="ECO:0000244|PDB:2ZP2"
FT   STRAND          221..226
FT                   /evidence="ECO:0000244|PDB:2ZP2"
SQ   SEQUENCE   240 AA;  26720 MW;  CFD927E3A8E0FF5F CRC64;
     MTVRYQIEQL GDSAMMIRFG EEINEQVNGI VHAAAAYIEE QPFPGFIECI PAFTSLTVFY
     DMYEVYKHLP QGISSPFESV KRDVEERLAE IAEDYEVNRR IVEIPVCYGG EFGPDLEEVA
     KINQLSPEEV IDIHTNGEYV VYMLGFAPGF PFLGGMSKRI AAPRKSSPRP SIPAGSVGIA
     GLQTGVYPIS TPGGWQLIGK TPLALFRPQE NPPTLLRAGD IVKFVRISEK DYHAYKEESN
//

If you have problems or comments...

PBIL Back to PBIL home page