PCP_ALIF1
ID PCP_ALIF1 Reviewed; 212 AA.
AC Q5E531;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Pyrrolidone-carboxylate peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE EC=3.4.19.3 {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=5-oxoprolyl-peptidase {ECO:0000255|HAMAP-Rule:MF_00417};
DE AltName: Full=Pyroglutamyl-peptidase I {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=PGP-I {ECO:0000255|HAMAP-Rule:MF_00417};
DE Short=Pyrase {ECO:0000255|HAMAP-Rule:MF_00417};
GN Name=pcp {ECO:0000255|HAMAP-Rule:MF_00417}; OrderedLocusNames=VF_1370;
OS Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=312309;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700601 / ES114;
RX PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT pathogenic congeners.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC -!- FUNCTION: Removes 5-oxoproline from various penultimate amino acid
CC residues except L-proline. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal pyroglutamyl group from a
CC polypeptide, the second amino acid generally not being Pro.;
CC EC=3.4.19.3; Evidence={ECO:0000255|HAMAP-Rule:MF_00417};
CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00417}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00417}.
CC -!- SIMILARITY: Belongs to the peptidase C15 family. {ECO:0000255|HAMAP-
CC Rule:MF_00417}.
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DR EMBL; CP000020; AAW85865.1; -; Genomic_DNA.
DR RefSeq; WP_005419351.1; NC_006840.2.
DR RefSeq; YP_204753.1; NC_006840.2.
DR AlphaFoldDB; Q5E531; -.
DR SMR; Q5E531; -.
DR STRING; 312309.VF_1370; -.
DR MEROPS; C15.001; -.
DR EnsemblBacteria; AAW85865; AAW85865; VF_1370.
DR KEGG; vfi:VF_1370; -.
DR PATRIC; fig|312309.11.peg.1379; -.
DR eggNOG; COG2039; Bacteria.
DR HOGENOM; CLU_043960_4_0_6; -.
DR OMA; KLAYNHK; -.
DR OrthoDB; 1927224at2; -.
DR Proteomes; UP000000537; Chromosome I.
DR GO; GO:0005829; C:cytosol; IEA:InterPro.
DR GO; GO:0016920; F:pyroglutamyl-peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00501; Peptidase_C15; 1.
DR Gene3D; 3.40.630.20; -; 1.
DR HAMAP; MF_00417; Pyrrolid_peptidase; 1.
DR InterPro; IPR000816; Peptidase_C15.
DR InterPro; IPR016125; Peptidase_C15-like.
DR InterPro; IPR036440; Peptidase_C15-like_sf.
DR InterPro; IPR029762; PGP-I_bact-type.
DR InterPro; IPR033694; PGPEP1_Cys_AS.
DR PANTHER; PTHR23402; PTHR23402; 1.
DR Pfam; PF01470; Peptidase_C15; 1.
DR PIRSF; PIRSF015592; Prld-crbxl_pptds; 1.
DR PRINTS; PR00706; PYROGLUPTASE.
DR SUPFAM; SSF53182; SSF53182; 1.
DR TIGRFAMs; TIGR00504; pyro_pdase; 1.
DR PROSITE; PS01334; PYRASE_CYS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Protease; Reference proteome; Thiol protease.
FT CHAIN 1..212
FT /note="Pyrrolidone-carboxylate peptidase"
FT /id="PRO_1000050153"
FT ACT_SITE 80
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 143
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
FT ACT_SITE 165
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00417"
SQ SEQUENCE 212 AA; 22804 MW; 551C6B9ADDCFF350 CRC64;
MKKILITGFE PFGNDKINPA LEAVKLIAGR KLNGGEIVIC QVPVVRYKSI ETVKQAIEEQ
QPYAVITVGQ ASGRAAITPE RIAINVDDFR IPDNEGIQVI DEPVVAGGPD AYFTTLPIKA
MVSEIQAQGI PATVSNTAGT FVCNHLFYGI QHYLKDTNVR HGFVHIPLLP EQSVDGSQPT
MKLEQIAEGL AIAAQAIIDN DSDIQQGAGT IC