ID   F0B813_9XANT            Unreviewed;       716 AA.
AC   F0B813;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   13-SEP-2023, entry version 52.
DE   SubName: Full=Peptidyl-dipeptidase Dcp {ECO:0000313|EMBL:EGD11399.1};
DE            EC=3.4.15.5 {ECO:0000313|EMBL:EGD11399.1};
GN   ORFNames=XVE_0209 {ECO:0000313|EMBL:EGD11399.1};
OS   Xanthomonas vesicatoria ATCC 35937.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=925775 {ECO:0000313|EMBL:EGD11399.1, ECO:0000313|Proteomes:UP000003299};
RN   [1] {ECO:0000313|EMBL:EGD11399.1, ECO:0000313|Proteomes:UP000003299}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35937 {ECO:0000313|EMBL:EGD11399.1,
RC   ECO:0000313|Proteomes:UP000003299};
RX   PubMed=21396108; DOI=10.1186/1471-2164-12-146;
RA   Potnis N., Krasileva K., Chow V., Almeida N.F., Patil P.B., Ryan R.P.,
RA   Sharlach M., Behlau F., Dow J.M., Momol M.T., White F.F., Preston J.F.,
RA   Vinatzer B.A., Koebnik R., Setubal J.C., Norman D.J., Staskawicz B.J.,
RA   Jones J.B.;
RT   "Comparative genomics reveals diversity among xanthomonads infecting tomato
RT   and pepper.";
RL   BMC Genomics 12:146-146(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|ARBA:ARBA00006040, ECO:0000256|RuleBase:RU003435}.
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:EGD11399.1}.
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DR   EMBL; AEQV01000004; EGD11399.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0B813; -.
DR   KEGG; xve:BJD12_20705; -.
DR   eggNOG; COG0339; Bacteria.
DR   Proteomes; UP000003299; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06456; M3A_DCP; 1.
DR   Gene3D; 1.10.1370.40; -; 1.
DR   Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR   Gene3D; 1.10.1370.10; Neurolysin, domain 3; 1.
DR   InterPro; IPR034005; M3A_DCP.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   InterPro; IPR024077; Neurolysin/TOP_dom2.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR43660; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR43660:SF1; DIPEPTIDYL CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:EGD11399.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          244..698
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
FT   REGION          697..716
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   716 AA;  78987 MW;  96C19D3FA84FDDF0 CRC64;
     MPSYSIAAPA TTQAATQGNP FFADSTLPLH YPQFDKIKDS DFAPAFDAGM AEQLKEVDKI
     ANQKAKPSFE NTIVALEKSG ATLDRATTVF FNLVGADTND ARKKLQADYS AKFAAHRDAI
     SLNGKLFARI QSLYDQRAKL GLDAQGLRLV EKYYSDFVRD GAKLSDADKT TLKAMNAELA
     NLGTTFSQNV LAEVNAAAVV VDDVKQLDGL SEEQIAAAAE AAKTRKLDGK YVIALLNTTG
     QPPLTQLKNR ELRKKIYDAS VSRGSHGGQY DNTALVSRIM KLRADKAKLL GFPTYAAYSL
     ENQTAKTPEA VNAMLGKLAP AAVANAKREA ADLQAMIDKE QKAARKPTFK LEAWDWAYYS
     EKVRQAKYNF DESQLKPYFE LKNVLENGVF YAANQEYGLT FKQRTDLPTY RDDITVYDVF
     DADGKQLAIF IADMYARESK RGGAWMNSYV SQSDLTGFKP VVANHLNIPK PPAGQPTLLT
     WDEVTTMFHE FGHALHGMFS DVKYPYFSGT SVPRDFVEFP SQVNEMWADE PSILKNYAKH
     YQNGTPMPQA LLDKVIAASK FNQGFATTEY LGAAMLDQNW HQISASQVPD PAGVMAFEAK
     ALQQDGIAYA PVPPRYKTPY FSHIMGGYAA GYYAYIWSEV LDANTQQWFK QHGGLSRANG
     DRFRQTLLSR GGSVDAMELF QNFAGHAPQI EPLLEKRGLS ANGGDGATPE APQSKP
//