PXPC_BACSU
ID PXPC_BACSU Reviewed; 335 AA.
AC Q7WY77; P42967;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=5-oxoprolinase subunit C {ECO:0000305};
DE Short=5-OPase subunit C {ECO:0000305};
DE EC=3.5.2.9 {ECO:0000269|PubMed:28830929};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit C {ECO:0000305};
DE AltName: Full=KipI antagonist;
DE AltName: Full=Protein KipA;
GN Name=pxpC {ECO:0000303|PubMed:28830929};
GN Synonyms=kipA {ECO:0000303|PubMed:9334321}; OrderedLocusNames=BSU04090;
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 SEQUENCE REVISION TO 172-217; 240; 242; 250; 256-270 AND 274-280.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [6]
RP FUNCTION, PROBABLE INTERACTION WITH PXPB, 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 [7]
RP INTERACTION WITH PXPB.
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).
RN [8]
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).
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, counteracts the inhibitory action of
CC PxpB (KipI) on sporulation, by binding to PxpB and preventing its
CC function as an inhibitor of kinase A (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 PxpB (PubMed:9334321,
CC PubMed:21050859, PubMed:28830929). {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: Disruption of the gene decreases 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 PxpC 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07361.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA09039.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D38161; BAA07361.1; ALT_FRAME; Genomic_DNA.
DR EMBL; D50453; BAA09039.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAE01447.2; -; Genomic_DNA.
DR PIR; G69765; G69765.
DR RefSeq; WP_003234419.1; NZ_JNCM01000031.1.
DR RefSeq; YP_054571.2; NC_000964.3.
DR AlphaFoldDB; Q7WY77; -.
DR SMR; Q7WY77; -.
DR STRING; 224308.BSU04090; -.
DR PaxDb; Q7WY77; -.
DR PRIDE; Q7WY77; -.
DR EnsemblBacteria; CAE01447; CAE01447; BSU_04090.
DR GeneID; 2914204; -.
DR KEGG; bsu:BSU04090; -.
DR PATRIC; fig|224308.43.peg.426; -.
DR eggNOG; COG1984; Bacteria.
DR InParanoid; Q7WY77; -.
DR OMA; QDLGRSH; -.
DR PhylomeDB; Q7WY77; -.
DR BioCyc; BSUB:BSU04090-MON; -.
DR BRENDA; 3.5.2.9; 658.
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:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR Pfam; PF02626; CT_A_B; 1.
DR SMART; SM00797; AHS2; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR TIGRFAMs; TIGR00724; urea_amlyse_rel; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome;
KW Sporulation.
FT CHAIN 1..335
FT /note="5-oxoprolinase subunit C"
FT /id="PRO_0000084307"
FT CONFLICT 172..217
FT /note="GKQGFAAPKWSVSRGRFLPLKKNPVIRVLEGKQFAFFTEESKTRFY -> AH
FT TVIGSTDVVSQPWEISVIEDESRHSSAGGISICLLHSRIKNAFS (in Ref. 1;
FT BAA07361 and 2; BAA09039)"
FT /evidence="ECO:0000305"
FT CONFLICT 240..242
FT /note="ELK -> DLT (in Ref. 1; BAA07361 and 2; BAA09039)"
FT /evidence="ECO:0000305"
FT CONFLICT 250
FT /note="E -> A (in Ref. 1; BAA07361 and 2; BAA09039)"
FT /evidence="ECO:0000305"
FT CONFLICT 256..270
FT /note="TVQVPPDGNPIILLA -> AAQMPPAGKPYYPCLQ (in Ref. 1;
FT BAA07361 and 2; BAA09039)"
FT /evidence="ECO:0000305"
FT CONFLICT 274..280
FT /note="TTGGYPR -> DDWPAIRG (in Ref. 1; BAA07361 and 2;
FT BAA09039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 335 AA; 36699 MW; 1DE5AB1FD4A93D79 CRC64;
MKVLKPGLLT TVQDIGRTGY QKYGVLASGA MDTVSLRIAN LLIGNGENEA GLEITMMGPG
PSFHFSKQTL IAVTGADFTL RINDEEAPLW KPVLIKENST VSFGPCKLGS RAYLAAAGGI
EVPAVMESKS TYVRGSIGGL HGRALQKEDE LNIGEMSALS QTILSRLSSQ LGKQGFAAPK
WSVSRGRFLP LKKNPVIRVL EGKQFAFFTE ESKTRFYEEA FRVTPQSDRM GYRLKGEPLE
LKAPLEMVSE AVSFGTVQVP PDGNPIILLA DRQTTGGYPR IAHIISADLP IVSQIMPGEH
VQFEPVSLQE AEALAVEREQ HIKELKTRMK MEWLT
