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Database: UniProt
Entry: A0A2T4U397_9BACI
LinkDB: A0A2T4U397_9BACI
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ID   A0A2T4U397_9BACI        Unreviewed;       414 AA.
AC   A0A2T4U397;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|SMART:SM00631};
GN   ORFNames=C6Y45_14510 {ECO:0000313|EMBL:PTL37825.1};
OS   Alkalicoccus saliphilus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalicoccus.
OX   NCBI_TaxID=200989 {ECO:0000313|EMBL:PTL37825.1, ECO:0000313|Proteomes:UP000240509};
RN   [1] {ECO:0000313|EMBL:PTL37825.1, ECO:0000313|Proteomes:UP000240509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6AG {ECO:0000313|EMBL:PTL37825.1,
RC   ECO:0000313|Proteomes:UP000240509};
RA   Zhao B.;
RT   "Alkalicoccus saliphilus sp. nov., isolated from a mineral pool.";
RL   Submitted (MAR-2018) 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:PTL37825.1}.
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DR   EMBL; PZJJ01000032; PTL37825.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T4U397; -.
DR   Proteomes; UP000240509; 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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..414
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015766265"
FT   DOMAIN          50..306
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   414 AA;  46466 MW;  7E9A12E91289CDDC CRC64;
     MITLKKVIFS ALAAPLLLTT VLPASAGAEP QSKPNGPWIQ PEQQTKLERF ISPEKMHEQL
     EEIEERARDG RMDLDVVGQS AKYDHPIYAV KFGESDTDNP KVYLQTQIHG DEQGGTEAAL
     DLIQTLAMSN NQDVRTILDN VTVWIVPMLN PDGAEIIERE EGQAKQRRNF QEWTPEEWGL
     SEDTPAPWYH GRDWASEELG FDVNRDFHPD LSFELTEEDA GLLPGVGSEP GFYVTPEAQA
     SRDVFAELEP DLFIDHHHRY SNTVSEDDDR LNTLQILGQV VDEDNVVSHN GTDYQLSEES
     LELSKQVNSH VYQVLQKGNS PFGAVSRYPD VNLPGTALGS FSLNDAAIML YETRGQQHPN
     GHTGQKSSGM LIKQSYIGIY ETLLGLATEE IYDIDPEFYD TEIPTDSPRI QRPE
//
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