ID A0A2I0SEN3_9ACTN Unreviewed; 454 AA.
AC A0A2I0SEN3;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:PKT68394.1};
GN ORFNames=CW362_35120 {ECO:0000313|EMBL:PKT68394.1};
OS Streptomyces populi.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2058924 {ECO:0000313|EMBL:PKT68394.1, ECO:0000313|Proteomes:UP000236178};
RN [1] {ECO:0000313|EMBL:PKT68394.1, ECO:0000313|Proteomes:UP000236178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A249 {ECO:0000313|EMBL:PKT68394.1,
RC ECO:0000313|Proteomes:UP000236178};
RA Wang Z.;
RT "Streptomyces populusis sp. nov., a novel endophytic actinobacterium
RT isolated from stems of Populus adenopoda Maxim.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M14 family.
CC {ECO:0000256|ARBA:ARBA00005988}.
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:PKT68394.1}.
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DR EMBL; PJOS01000112; PKT68394.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0SEN3; -.
DR OrthoDB; 5240362at2; -.
DR Proteomes; UP000236178; Unassembled WGS sequence.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd03859; M14_CPT; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR033810; Carboxypeptidase_T.
DR InterPro; IPR000834; Peptidase_M14.
DR PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:PKT68394.1};
KW Hydrolase {ECO:0000313|EMBL:PKT68394.1};
KW Protease {ECO:0000313|EMBL:PKT68394.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236178};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..454
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039033035"
FT DOMAIN 186..208
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00132"
FT DOMAIN 330..340
FT /note="Peptidase M14 carboxypeptidase A"
FT /evidence="ECO:0000259|PROSITE:PS00133"
SQ SEQUENCE 454 AA; 49349 MW; BCD4C43678514BFF CRC64;
MRIRPRGSAD GKGRGGRRTA ALAVLAALAL AAPLTATATD ATASGATALK PSSDDIRQYE
IHQSSNSASR TEIQRSGVTV DEADEETVVV SGRADQIATL RRQGYDVTPL GSAPDRSSAA
DDVRLFDFPT ADAKYHNYAE MNAEIDQRLA AYPSIMSKRV IGKSYQGRDI VAIKVSDNVA
TDESEPEVLL TFHQHAREHL TVEMALYLLR ELGAGYGSDS RVTNMVNNRE IWIVPDLNPD
GGEYDIASGS YRSWRKNRQP NSGSSYVGTD LNRNWNYKWG CCGGSSSSKS SETYRGASAE
SAPEVKVVAD FVRGRVVGGK QQITAGIDFH TYSELVLWPF GYTTADTATG MTADDAAAFK
AIGQKMAASN GYTAEQASDL YITDGSIDDY LWGTQKIFDY TFEMYPTSSS GGGFYPPDEV
IERETSRNRD AVLQLLENAD CMYRSIGKAA QYCS
//
