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Database: UniProt
Entry: A0A2C6CW65_9BACT
LinkDB: A0A2C6CW65_9BACT
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ID   A0A2C6CW65_9BACT        Unreviewed;       573 AA.
AC   A0A2C6CW65;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|PROSITE:PS00133};
GN   ORFNames=CEQ90_09045 {ECO:0000313|EMBL:PHI20322.1};
OS   Lewinellaceae bacterium SD302.
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Lewinellaceae.
OX   NCBI_TaxID=2014804 {ECO:0000313|EMBL:PHI20322.1, ECO:0000313|Proteomes:UP000223945};
RN   [1] {ECO:0000313|EMBL:PHI20322.1, ECO:0000313|Proteomes:UP000223945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SD302 {ECO:0000313|EMBL:PHI20322.1,
RC   ECO:0000313|Proteomes:UP000223945};
RA   Wang K.;
RT   "The draft genome sequence of Lewinellaceae bacterium SD302.";
RL   Submitted (JUL-2017) to the EMBL/GenBank/DDBJ databases.
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:PHI20322.1}.
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DR   EMBL; PDLQ01000010; PHI20322.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C6CW65; -.
DR   OrthoDB; 1652165at2; -.
DR   Proteomes; UP000223945; 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; cd18173; M14_CP_bacteria; 1.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11532:SF57; PEPTIDASE_M14 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR11532; PROTEASE M14 CARBOXYPEPTIDASE; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   PRINTS; PR00765; CRBOXYPTASEA.
DR   SMART; SM00631; Zn_pept; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00133; CARBOXYPEPT_ZN_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000223945}.
FT   DOMAIN          287..297
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|PROSITE:PS00133"
SQ   SEQUENCE   573 AA;  64585 MW;  15A95E1E354DE38D CRC64;
     MRFYRFLLSL LLVAILAGGD LLSQTGRQIN SADEQQFRVE VRASANQLLR QEGYTPDHGS
     NATVTYVIGG RELIELLRRS GYQPSVEPID GVEVATVTLQ EVQSRLSADN CFVPLDAYPS
     YALYESLLEG FADNYPEIAR IHELGVLASG RRILALEITD QPDEEEAEPK VLLTSSMHGD
     ELGGFHVSLR LISELVCNYG NDVELTNLIN TTEIWINPLA NPDGTYRDDN TIISEPTRGN
     ANFIDLNRNF PDPDNGDHPD GNAYQPETEI FMQFAEDYAF DLSLNIHGGA EVFNYPWDTY
     AQRTADDNWW KHIARQYADS CQHTAGHNGY MDALNNGITN GYDWYPIYGG RQDYTTYFHH
     GREATLEISN IKTTPPEQFE FIWNANRRPL INFIKQAGYG LRGVVRDSLT AAPLGASVFI
     DGHDEYNSDV YSKMPTGRYH RYLKAGIYNV LFSAEGYHPK LVACFVGDDE PTFKDVNLLP
     IQSSNSTLAD SELITAFYQS GSLYLDHLPE DHHNWHLELL SVDGRRITTS GIPGGRRRFN
     LRVGYLAPGA YICRVHENGK QRVLRFSSVV RKK
//
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