ID   A0A098F505_9BACI        Unreviewed;       879 AA.
AC   A0A098F505;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Peptidase M14 carboxypeptidase A {ECO:0000313|EMBL:CEG28737.1};
GN   ORFNames=BN1002_03660 {ECO:0000313|EMBL:CEG28737.1};
OS   Bacillus sp. B-jedd.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1476857 {ECO:0000313|EMBL:CEG28737.1, ECO:0000313|Proteomes:UP000042335};
RN   [1] {ECO:0000313|EMBL:CEG28737.1, ECO:0000313|Proteomes:UP000042335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B-jedd {ECO:0000313|EMBL:CEG28737.1,
RC   ECO:0000313|Proteomes:UP000042335};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (SEP-2014) 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; CCXR01000001; CEG28737.1; -; Genomic_DNA.
DR   RefSeq; WP_048826807.1; NZ_CCXR01000001.1.
DR   AlphaFoldDB; A0A098F505; -.
DR   OrthoDB; 9809277at2; -.
DR   Proteomes; UP000042335; 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; 3.50.30.30; -; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR046450; PA_dom_sf.
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; SSF52025; PA domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:CEG28737.1};
KW   Hydrolase {ECO:0000313|EMBL:CEG28737.1};
KW   Protease {ECO:0000313|EMBL:CEG28737.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000042335};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           31..879
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001941582"
FT   DOMAIN          189..482
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|SMART:SM00631"
SQ   SEQUENCE   879 AA;  96364 MW;  95C088191257020D CRC64;
     MLKASSKNTK LKVFLTSVLI ICLAFPTVFA AANDSAAGQV PFVKTPGTFP IVEVTVTGVE
     ALEALFAEEL DLDIFGYDHD GDEFTVTIQI HNDELEYFEK NNISYEVVDD GTWIFEKPST
     KGGKSAKSVM NASAEGQPIP GLPERANASP TVNSPLPLPI TAPIEPDAVF DPTGVSFNAR
     WGFPDRLGYR TVTEFYAEMN YLAAKYPELV KLHEYGVSFE GVPLRALEIS NNPGGNDGRP
     TTLHQAGNHA REYNTSELAM NLGWYLLTKY GKAGHEEVTK LLDTTSVWIL PMTNPDGVHW
     DMRNSPGSWR YNRNNYAGTE HNPDGTIIGG VDLNRNYAYG WGSINGSQSF FGQGNFRGGA
     PLSEPEIMAV SEVLRSNMVV SSLSGHSFPN GNGQLVVYPW AFVLNTFSYD DNREFPIQIT
     DTVSVKDLGR RQGNYNLYSD EFTNGMYAYS GESLDYKLGA LRTLGFLYEF GRTLLPKYTG
     ADQYYAVAPY KDQYFEEPRE FLLTYPTAAN AVGAGAPSAD ISAQVVFLNA PYDGGYGRSR
     FTTVEQVNAL GTELDGKILV TTRANANNDN AAIAIAAQNL GAVGVIMVDE NAFPHGYGYR
     HFNPNLGNGT TAGVNRPADV SIPVAGTSKP YVRELNERIG SGKLTIKSTT TNQESMVWTF
     ERNIGAFMEN MSFAVEFSSH IKGKITDKAG RLVPEATLKL EKEVVSPLIE GNTGLNEEAT
     RDRITQSGEF RQQQTAVYEA KGGLYDWSVT PSKQLDNPLV HGTPIVDEGY TITVSAPGKE
     SVTKKNVKIP SYQSTIELDF ELLSLPKETK ASAFVTKLKG SQNDLTITVT EKYTDGYVNV
     VTETIRINNN ATGTYEVGDN MVYVDTKGDT QIRECYVVE
//