ID   PXPA_CAMJE              Reviewed;         255 AA.
AC   Q9PMC8; Q0P884;
DT   04-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE            Short=5-OPase subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
DE            EC=3.5.2.9 {ECO:0000255|HAMAP-Rule:MF_00691};
DE   AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000255|HAMAP-Rule:MF_00691};
GN   Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691}; OrderedLocusNames=Cj1541;
OS   Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS   11168).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=192222;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700819 / NCTC 11168;
RX   PubMed=10688204; DOI=10.1038/35001088;
RA   Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA   Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA   Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA   Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA   Barrell B.G.;
RT   "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT   reveals hypervariable sequences.";
RL   Nature 403:665-668(2000).
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       {ECO:0000255|HAMAP-Rule:MF_00691}.
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:0000255|HAMAP-Rule:MF_00691};
CC   -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC       {ECO:0000255|HAMAP-Rule:MF_00691}.
CC   -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00691}.
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DR   EMBL; AL111168; CAL35641.1; -; Genomic_DNA.
DR   PIR; C81301; C81301.
DR   RefSeq; WP_002851457.1; NC_002163.1.
DR   RefSeq; YP_002344913.1; NC_002163.1.
DR   AlphaFoldDB; Q9PMC8; -.
DR   SMR; Q9PMC8; -.
DR   IntAct; Q9PMC8; 6.
DR   STRING; 192222.Cj1541; -.
DR   PaxDb; Q9PMC8; -.
DR   PRIDE; Q9PMC8; -.
DR   EnsemblBacteria; CAL35641; CAL35641; Cj1541.
DR   GeneID; 905823; -.
DR   KEGG; cje:Cj1541; -.
DR   PATRIC; fig|192222.6.peg.1518; -.
DR   eggNOG; COG1540; Bacteria.
DR   HOGENOM; CLU_069535_0_0_7; -.
DR   OMA; DRTYKQD; -.
DR   Proteomes; UP000000799; Chromosome.
DR   GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   HAMAP; MF_00691; PxpA; 1.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR005501; LamB/YcsF/PxpA-like.
DR   PANTHER; PTHR30292; PTHR30292; 1.
DR   Pfam; PF03746; LamB_YcsF; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..255
FT                   /note="5-oxoprolinase subunit A"
FT                   /id="PRO_0000185000"
SQ   SEQUENCE   255 AA;  28084 MW;  4D10A0B1BBEA122A CRC64;
     MFKVDLNSDL GESFGAYKMG MDEEILKFVS SVNVACGFHA GDPCVMDETL NLAKQNGVCI
     GAHPSYPDLL GFGRRNMQIS FEEAKNYALY QLGALFGFAK AKGMKIQHFK AHGALYNMAA
     IDENLALALC EAVASFDENI IFLGLSNSAM NEAAKKKGLR YANEVFADRA YNDDGTLVSR
     KLEGALIHDE NLAIKRVIKM IKESKVTSIN GKEIDLKADS ICVHGDNAKA LEFVKKIKEN
     LKKEQIQICA LENFI