ID   R5F0W1_9FIRM            Unreviewed;       456 AA.
AC   R5F0W1;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Dipeptidase PepV {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN466_00363 {ECO:0000313|EMBL:CCX93911.1};
OS   Firmicutes bacterium CAG:110.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263000 {ECO:0000313|EMBL:CCX93911.1, ECO:0000313|Proteomes:UP000018021};
RN   [1] {ECO:0000313|EMBL:CCX93911.1, ECO:0000313|Proteomes:UP000018021}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:110 {ECO:0000313|Proteomes:UP000018021};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
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:CCX93911.1}.
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DR   EMBL; CAXG010000438; CCX93911.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5F0W1; -.
DR   Proteomes; UP000018021; Unassembled WGS sequence.
DR   GO; GO:0016805; F:dipeptidase 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; IPR002933; Peptidase_M20.
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};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protease {ECO:0000256|ARBA:ARBA00022997};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018021};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
SQ   SEQUENCE   456 AA;  48592 MW;  781A6A7394F3A513 CRC64;
     MELRACVDAL KPQLLSTLRQ NIQIPSVQGE AEDGAPYGAS VRESLVHVLD TARELGFRTE
     NMDGHLGWCE YGEGDEMVAV LGHLDVVPAG DGWSCDPFGG ELQDGKIWGR GTTDDKGPAV
     ASLFALAALR DSGLPIRRRI RILFGCNEEA GSDDIKYYLA NGGEIPVMGF TPDGEYPVIN
     GEKGIINVTF SHANVQTGDV RLLSIHGGTA PNVVPAHACA KLACPRELAQ RLANLSAPQV
     RFTATDYGLF VEAEGESAHG STPELGKNAI GRLLLALDTL PLSGEVANAV HFLAATLGME
     TDGASAGIAL HDAVSGGLTL NLGVINGDEH RLSLKINYRY PVTKGYADCA PILNGKFASA
     GFTLDSEVHK AKLYVPEDSP LVSTLLRVYR EQTGLEDQPK SIGGGTYAKA LPNIVAFGPI
     FPGEEVREHK PDEYISVDSL MRNAQIIAAA MYEMAK
//