PXPC_ECOLI
ID PXPC_ECOLI Reviewed; 310 AA.
AC P75745;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
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};
GN Name=pxpC {ECO:0000303|PubMed:28830929}; Synonyms=ybgK;
GN OrderedLocusNames=b0712, JW0702;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, 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 [5] {ECO:0007744|PDB:5DUD}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS).
RA Arbing M.A., Kaufmann M., Shin A., Medrano-Soto A., Cascio D.,
RA Eisenberg D.;
RT "Crystal structure of E. coli YbgJK.";
RL Submitted (SEP-2015) to the PDB data bank.
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:0000269|PubMed:28830929}.
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 {ECO:0000250|UniProtKB:Q7WY77}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene slows growth on minimal
CC medium with ammonium as nitrogen source. {ECO:0000269|PubMed:28830929}.
CC -!- SIMILARITY: Belongs to the PxpC family. {ECO:0000305}.
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DR EMBL; U00096; AAC73806.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35376.1; -; Genomic_DNA.
DR PIR; G64806; G64806.
DR RefSeq; NP_415240.1; NC_000913.3.
DR RefSeq; WP_000912724.1; NZ_SSZK01000033.1.
DR PDB; 5DUD; X-ray; 2.80 A; A/C=1-310.
DR PDBsum; 5DUD; -.
DR AlphaFoldDB; P75745; -.
DR SMR; P75745; -.
DR BioGRID; 4259922; 246.
DR BioGRID; 849693; 1.
DR DIP; DIP-11397N; -.
DR IntAct; P75745; 7.
DR STRING; 511145.b0712; -.
DR jPOST; P75745; -.
DR PaxDb; P75745; -.
DR PRIDE; P75745; -.
DR EnsemblBacteria; AAC73806; AAC73806; b0712.
DR EnsemblBacteria; BAA35376; BAA35376; BAA35376.
DR GeneID; 945317; -.
DR KEGG; ecj:JW0702; -.
DR KEGG; eco:b0712; -.
DR PATRIC; fig|1411691.4.peg.1561; -.
DR EchoBASE; EB3091; -.
DR eggNOG; COG1984; Bacteria.
DR HOGENOM; CLU_028967_0_3_6; -.
DR InParanoid; P75745; -.
DR OMA; QDLGRSH; -.
DR PhylomeDB; P75745; -.
DR BioCyc; EcoCyc:G6381-MON; -.
DR BioCyc; MetaCyc:G6381-MON; -.
DR PRO; PR:P75745; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..310
FT /note="5-oxoprolinase subunit C"
FT /id="PRO_0000168709"
FT STRAND 2..5
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5DUD"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:5DUD"
FT HELIX 34..44
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 52..57
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 68..75
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 99..102
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 109..115
FT /evidence="ECO:0007829|PDB:5DUD"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:5DUD"
FT TURN 138..141
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 172..178
FT /evidence="ECO:0007829|PDB:5DUD"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:5DUD"
FT HELIX 187..195
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 198..200
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 206..213
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 251..253
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:5DUD"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:5DUD"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:5DUD"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:5DUD"
FT HELIX 285..302
FT /evidence="ECO:0007829|PDB:5DUD"
SQ SEQUENCE 310 AA; 34386 MW; 998FDFEB23602C25 CRC64;
MLKIIRAGMY TTVQDGGRHG FRQSGISHCG ALDMPALRIA NLLVGNDANA PALEITLGQL
TVEFETDGWF ALTGAGCEAR LDDNAVWTGW RLPMKAGQRL TLKRPQHGMR SYLAVAGGID
VPPVMGSCST DLKVGIGGLE GRLLKDGDRL PIGKSKRDSM EAQGVKQLLW GNRIRALPGP
EYHEFDRASQ DAFWRSPWQL SSQSNRMGYR LQGQILKRTT DRELLSHGLL PGVVQVPHNG
QPIVLMNDAQ TTGGYPRIAC IIEADMYHLA QIPLGQPIHF VQCSLEEALK ARQDQQRYFE
QLAWRLHNEN
