ID   PXPC_HAEIN              Reviewed;         309 AA.
AC   P44298;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=5-oxoprolinase subunit C {ECO:0000250|UniProtKB:P75745};
DE            Short=5-OPase subunit C {ECO:0000250|UniProtKB:P75745};
DE            EC=3.5.2.9 {ECO:0000250|UniProtKB:P75745};
DE   AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit C {ECO:0000250|UniProtKB:P75745};
GN   Name=pxpC {ECO:0000250|UniProtKB:P75745}; OrderedLocusNames=HI_1730;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
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:0000250|UniProtKB:P75745}.
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:0000250|UniProtKB:P75745};
CC   -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC       {ECO:0000250|UniProtKB:Q7WY77}.
CC   -!- SIMILARITY: Belongs to the PxpC family. {ECO:0000305}.
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DR   EMBL; L42023; AAC23376.1; -; Genomic_DNA.
DR   PIR; B64041; B64041.
DR   RefSeq; NP_439871.1; NC_000907.1.
DR   RefSeq; WP_005694216.1; NC_000907.1.
DR   AlphaFoldDB; P44298; -.
DR   SMR; P44298; -.
DR   STRING; 71421.HI_1730; -.
DR   PRIDE; P44298; -.
DR   EnsemblBacteria; AAC23376; AAC23376; HI_1730.
DR   KEGG; hin:HI_1730; -.
DR   PATRIC; fig|71421.8.peg.1809; -.
DR   eggNOG; COG1984; Bacteria.
DR   HOGENOM; CLU_028967_0_3_6; -.
DR   OMA; QDLGRSH; -.
DR   PhylomeDB; P44298; -.
DR   BioCyc; HINF71421:G1GJ1-1745-MON; -.
DR   Proteomes; UP000000579; 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   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   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..309
FT                   /note="5-oxoprolinase subunit C"
FT                   /id="PRO_0000168710"
SQ   SEQUENCE   309 AA;  34562 MW;  E34D87B4C838EF1D CRC64;
     MIDILDVKSR ATIQDLGRFG LRRFGISHCG AMDKLALRAG NILLGNAENV PAIEVPLGGI
     TLQFQQDMNF CVTGAFYEMM LDDKPVFAYW RYQVRAGQIL KMARAKIGMY GYLCVQGGFV
     LPQALNSCST DLRAQIGGIE GRCLQAGDQL QTANDHILRS EIGIAPIPLR DVIRALPSSE
     YQAFKRKSQY YWWRNEWTLQ SNSDRMGYRF QGQTLELKQP LEMLSHAIQF GSVQVPPSGQ
     PIILMADAQT TGGYPKIANV IDADLGALAQ VRLGSTIKFE AVSLQEAAKL RRKNEIYLDQ
     IRRIVDEKN