ID   G5KGL9_9STRE            Unreviewed;       468 AA.
AC   G5KGL9;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=Dipeptidase PepV {ECO:0000313|EMBL:EHJ57185.1};
DE            EC=3.4.13.- {ECO:0000313|EMBL:EHJ57185.1};
GN   Name=pepV {ECO:0000313|EMBL:EHJ57185.1};
GN   ORFNames=STRUR_1343 {ECO:0000313|EMBL:EHJ57185.1};
OS   Streptococcus urinalis 2285-97.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=764291 {ECO:0000313|EMBL:EHJ57185.1, ECO:0000313|Proteomes:UP000005388};
RN   [1] {ECO:0000313|EMBL:EHJ57185.1, ECO:0000313|Proteomes:UP000005388}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2285-97 {ECO:0000313|EMBL:EHJ57185.1};
RX   PubMed=24625962; DOI=10.1093/gbe/evu048;
RA   Richards V.P., Palmer S.R., Pavinski Bitar P.D., Qin X., Weinstock G.M.,
RA   Highlander S.K., Town C.D., Burne R.A., Stanhope M.J.;
RT   "Phylogenomics and the dynamic genome evolution of the genus
RT   Streptococcus.";
RL   Genome Biol. Evol. 6:741-753(2014).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EHJ57185.1}.
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DR   EMBL; AEUZ02000001; EHJ57185.1; -; Genomic_DNA.
DR   RefSeq; WP_006739907.1; NZ_AEUZ02000001.1.
DR   AlphaFoldDB; G5KGL9; -.
DR   STRING; 764291.STRUR_1343; -.
DR   eggNOG; COG0624; Bacteria.
DR   Proteomes; UP000005388; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   CDD; cd03888; M20_PepV; 1.
DR   Gene3D; 3.30.70.360; -; 2.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010964; M20A_pepV-rel.
DR   InterPro; IPR011291; Pept_M20A_peptidaseV.
DR   InterPro; IPR002933; Peptidase_M20.
DR   NCBIfam; TIGR01886; dipeptidase; 1.
DR   NCBIfam; TIGR01887; dipeptidaselike; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF33; DIPEPTIDASE SAOUHSC_01868-RELATED; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   4: Predicted;
KW   Dipeptidase {ECO:0000256|ARBA:ARBA00022997, ECO:0000313|EMBL:EHJ57185.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EHJ57185.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997, ECO:0000313|EMBL:EHJ57185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005388};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   468 AA;  51913 MW;  9890B770D0D6AEE4 CRC64;
     MTIDFKAEVA KRQDDLLEDL KSILRINSER DASKADKEHP FGPGPVKALE HFLEMAKRDG
     YQTRNIENYA GDFEFGQGDE VLGIFGHLDV VPAGSGWDTD PYEPVIKDNK IYARGSSDDK
     GPTLACYYAL KIIKELELPV SKKVRFIVGT DEESGWGDMD YYFAHNGLKD PDFGFSPDAE
     FPIINGEKGN ITEYLHFEGK NEGQYTLVSF KGGLRENMVP ESATAVIKAQ IELKELQEAL
     TDFCNQNHLT SEVNFENDQF TITINGKSAH GSTPEEGING ATFLAKFLSQ FAFSGPAKQY
     LNTAGNLIHE DFAGKNLGVA YEDAKMGALS MNAGVFQFDK ESNDNTIALN FRYPQGTDAD
     TIKSGLEKIN GLTKVTLSQH EHTPHYVPME DELVKTLLSV YEKQTGLEGH EQIIGGGTFG
     RLLKRGVAFG AMFPGDENTM HQANEYMPLD NIFRSAAIYA EAIYELIK
//