ID   A0A1B6AEG8_9ACTN        Unreviewed;       446 AA.
AC   A0A1B6AEG8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=Carboxypeptidase {ECO:0000313|EMBL:GAU65654.1};
GN   ORFNames=SSP35_02_00210 {ECO:0000313|EMBL:GAU65654.1};
OS   Streptomyces sp. NBRC 110611.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1621259 {ECO:0000313|EMBL:GAU65654.1, ECO:0000313|Proteomes:UP000094479};
RN   [1] {ECO:0000313|EMBL:GAU65654.1, ECO:0000313|Proteomes:UP000094479}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 110611 {ECO:0000313|EMBL:GAU65654.1,
RC   ECO:0000313|Proteomes:UP000094479};
RA   Igarashi Y., Komaki H., Ichikawa N., Hosoyama A., Fujita N., Panbangred W.;
RT   "Whole genome shotgun sequence of Streptomyces sp. NBRC 110611.";
RL   Submitted (MAR-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}.
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:GAU65654.1}.
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DR   EMBL; BBUY01000002; GAU65654.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B6AEG8; -.
DR   STRING; 1621259.GCA_001590865_00965; -.
DR   Proteomes; UP000094479; 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   Gene3D; 3.40.630.10; Zn peptidases; 1.
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   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:GAU65654.1};
KW   Hydrolase {ECO:0000313|EMBL:GAU65654.1};
KW   Protease {ECO:0000313|EMBL:GAU65654.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094479};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..446
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008578862"
FT   DOMAIN          54..280
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
FT   REGION          33..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  47640 MW;  DB599E707162FFAA CRC64;
     MTRRSRRPGR LLALGALAFG LTVTLGATLP AAPAGAAGTP TPRTGFETSH GTRWTSQPEE
     QAFLAAVDRA SARVRVDRIG TTEQGRPLRL VRIGAPAPER PAGVRRGNSV LLICAQHGDE
     PSGREACLST VRDLAYARDR ATRRFLERTS VLVVPTANPD GRAANIRGNA DGKDINRDHL
     ALRTAEARAV ATVLRDYRPD SVLDLHEYDA VVPYYTKDLL SLWPRNPNTA EAVHHESGVL
     AGEFVGPAVR NAGFSTGVYG IWTDPETGEP VKQVAGDGQE RILRNTVGVK GSLGLLVETR
     INPLTAAEQA DPALNNRRRV DSQLAAVKGA FDFSGRHRAR VEAATATARL AGYADHGPVY
     LGGADNAPPT DAQTLSDPPC AYRLDAAQLA RIEDALALHG LVWRPDPAGG AVVPLRQSLR
     GLVPLLLDQR AGYHLAVAMP TDDCRA
//