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
//