ID W4SBU9_9XANT Unreviewed; 732 AA.
AC W4SBU9;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Peptidyl-dipeptidase dcp {ECO:0000313|EMBL:GAE53658.1};
GN ORFNames=XPR_0293 {ECO:0000313|EMBL:GAE53658.1};
OS Xanthomonas arboricola pv. pruni MAFF 301420.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=1418095 {ECO:0000313|EMBL:GAE53658.1, ECO:0000313|Proteomes:UP000019084};
RN [1] {ECO:0000313|EMBL:GAE53658.1, ECO:0000313|Proteomes:UP000019084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 301420 {ECO:0000313|Proteomes:UP000019084};
RA Fujikawa T., Nakazono-Nagaoka E.;
RT "Genome sequence and analysis of Xanthomonas arboricola pv. pruni.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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:GAE53658.1}.
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DR EMBL; BAVC01000018; GAE53658.1; -; Genomic_DNA.
DR AlphaFoldDB; W4SBU9; -.
DR Proteomes; UP000019084; Unassembled WGS sequence.
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; 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 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 Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..732
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004848633"
FT DOMAIN 260..714
FT /note="Peptidase M3A/M3B catalytic"
FT /evidence="ECO:0000259|Pfam:PF01432"
SQ SEQUENCE 732 AA; 80576 MW; FC6A500EDD038FA7 CRC64;
MTTRLAFALA ASLGLAMPSY SIAAPATTQA ATQGNPFFAD STLPLHYPQF DKITDSDFAP
AFNAGMTEQL KEVEKIANQK AKPSFDNTLI ALEKSGATLD RATTVFFNLV GADTNDARKK
LQADYSAKFA AHRDAISLNG KLFARIQTLY DQRSKLGLDA QGVRLVEKYY SDFLRDGAKL
SDADKTTLKA MNAELANLGT TFSQNVLAEV NAAAVVVDDV KQLDGLSEEQ IAAAAEAAKA
RKLDGKYVIA LLNTTGQPPL TQLKNRELRK KIYDASVSRG SHGGQYDNTA LVARIMKLRA
DKAKLLGFPT YAAYSLENQT AKTPEAVNAM LGKLAPAAVA NAKREAADLQ AMIDKEQKAA
RKPTFKLEAW DWAYYSEKVR QAKYNFDESQ LKPYFELKNV LENGVFYAAN QEYGLTFKQR
TDLPTYRDDI TVYDVFDADG KQLAIFIADM YARESKRGGA WMNSYVSQSA LTGFRPVVAN
HLNIPKPPAG QPTLLTWDEV TTMFHEFGHA LHGMFSDVKY PYFSGTSVPR DFVEFPSQVN
EMWADEPSIL KNYAKHYQNG TPMPQVLLDK VIAASKFNQG FATTEYLGAA MLDQNWHQLS
ASQVPDAAGV MAFEAKALQQ DGIAYAPVPP RYKTPYFSHI MGGYAAGYYA YIWSEVLDAN
TQQWFKQHGG LSRANGDRFR QTLLSRGGSV DAMELFQNFA GHAPQIEPLL EKRGLSAQGG
DGATPEAPQS KP
//
