ID A0A0H5CTP7_9PSEU Unreviewed; 556 AA.
AC A0A0H5CTP7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carboxypeptidase T {ECO:0000313|EMBL:CRK61383.1};
DE EC=3.4.17.18 {ECO:0000313|EMBL:CRK61383.1};
OS Alloactinosynnema sp. L-07.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae.
OX NCBI_TaxID=1653480 {ECO:0000313|EMBL:CRK61383.1, ECO:0000313|Proteomes:UP000076116};
RN [1] {ECO:0000313|Proteomes:UP000076116}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L-07 {ECO:0000313|Proteomes:UP000076116};
RA Ramaraj T.;
RL Submitted (MAY-2015) 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}.
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DR EMBL; LN850107; CRK61383.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0H5CTP7; -.
DR STRING; 1653480.gene:80950281; -.
DR KEGG; alo:CRK61383; -.
DR Proteomes; UP000076116; Chromosome i.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03859; M14_CPT; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR033810; Carboxypeptidase_T.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR002884; P_dom.
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; PF01483; P_proprotein; 1.
DR Pfam; PF00246; Peptidase_M14; 1.
DR PRINTS; PR00765; CRBOXYPTASEA.
DR SMART; SM00631; Zn_pept; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00132; CARBOXYPEPT_ZN_1; 1.
DR PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
DR PROSITE; PS51829; P_HOMO_B; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CRK61383.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CRK61383.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000076116};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..556
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5005217073"
FT DOMAIN 436..556
FT /note="P/Homo B"
FT /evidence="ECO:0000259|PROSITE:PS51829"
SQ SEQUENCE 556 AA; 59966 MW; 53BEA7A6262D11B6 CRC64;
MNRKRLSVTV GALAAFAMVI SMNGGSAAGD KAAQTARASA EYHVTGVKTV QQRSAIAATG
AAINGTEDSR LLITATPGEV AKIRAQGFTV EAEAAPAVTQ GTQGANGVND FPSADAGYHN
YAEMNSVLNT AVANYPSIIS KQVIGKSYEN RDILAFKISD NVATDENEPE VLFTHHQHAR
EHLTVEMALY LVKTFTQGYA TDARIKGLVD SREIWILPDV NPDGGEFDIA TGSYRSWRKN
RQPNAGSSNV GTDMNRNWDY KWGCCNGSSG STGSETYRGT APESAKEVKV LSDFVRSRVV
GGTQQISVAI DFHTYSELVL WPFGWTYNDT APGLNAEEHN IFSTMGRAMA QTNGYTPEQA
SDLYITDGTI DDYLWGVHRI WGYTFEMFPS GAGGGGFYPG DEIIDRETAR NKAAVLYLLD
YADCPKRSIG LTCDGTPPPP GKVFENANNV NIPDSPAAAV FSDVVVSGVT GNAPATLKVD
VDIKHTWRGD LVIDLVAPDG SLYRLKNSSG NDSADNVIAT YTVNASTEVA NGTWRLKVQD
VARYDTGYID NFKLTF
//