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Database: UniProt
Entry: Q4ECB0_9RICK
LinkDB: Q4ECB0_9RICK
Original site: Q4ECB0_9RICK 
ID   Q4ECB0_9RICK            Unreviewed;       473 AA.
AC   Q4ECB0;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   13-SEP-2023, entry version 54.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=EA652_1224 {ECO:0000313|EMBL:QEF50891.1};
OS   Wolbachia endosymbiont of Drosophila ananassae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=307502 {ECO:0000313|EMBL:QEF50891.1, ECO:0000313|Proteomes:UP000321156};
RN   [1] {ECO:0000313|EMBL:QEF50891.1, ECO:0000313|Proteomes:UP000321156}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W2.1 {ECO:0000313|EMBL:QEF50891.1,
RC   ECO:0000313|Proteomes:UP000321156};
RA   Gasser M.T., Chung M., Bromley R.E., Nadendla S., Dunning Hotopp J.C.;
RT   "Complete Genome of Wolbachia endosymbiont, wAna, from Drosophila
RT   ananassae.";
RL   Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC       sequentially from the C-terminus, including neutral, aromatic, polar
CC       and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of a C-terminal amino acid with broad specificity,
CC         except for -Pro.; EC=3.4.17.19;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC   -!- SIMILARITY: Belongs to the peptidase M32 family.
CC       {ECO:0000256|PIRNR:PIRNR006615}.
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DR   EMBL; CP042904; QEF50891.1; -; Genomic_DNA.
DR   RefSeq; WP_007548790.1; NZ_NSDT01000057.1.
DR   KEGG; wea:EA652_1224; -.
DR   OrthoDB; 9772308at2; -.
DR   Proteomes; UP000321156; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02074; Peptidase_M32; 1.
DR   PIRSF; PIRSF006615; Zn_crbxpep_Taq; 2.
DR   PRINTS; PR00998; CRBOXYPTASET.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000313|EMBL:QEF50891.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW   Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW   ECO:0000256|PIRSR:PIRSR006615-1};
KW   Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW   Protease {ECO:0000256|PIRNR:PIRNR006615};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   BINDING         268
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   473 AA;  54558 MW;  0206D56905582B52 CRC64;
     MQSYKFLEEV LYRVKNIENT LKVLNQSQLN IEDKVEQMSL LEEIRHEIIS HDAIKESLAD
     ALGNKKSANT QQLKLIERIH KSNSAVPIDL VKSLSKAKVE CQDLWKLSHS ETSNLEKLKE
     RFTDLITLIR EVASIKSQQL KCSKYDSLLA DYDSDITEKN IREVFPKVGK FFSENVDKII
     EKQKKDKVTN IQKVATQKQI ELGSLCLQQM GIALNEIRTS YYYPIDYDES DFCYGLFSLL
     RHSGYAIYQK CLAQNSISSP ITRHVMYETQ GLFMERMIGT SREFIEFIQP HIKEKFAIKG
     KTNEKVSSVE NLYLIFNEIN LSSFLKNADE FSLLAHIMLR TRLEQDIING TLEVKDLHDA
     WLEGMKHYKI PVKAENELNT YFQDEYWASG VMGYFPIKII ALIAAVQIFS FVKKNHYESL
     SAIIKGDFSL LISWLSQNVY SAKCGLELLK KVTGKGLDVE CVTYYLSEKY NLS
//
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