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Database: UniProt
Entry: A0A1I7F002_9FLAO
LinkDB: A0A1I7F002_9FLAO
Original site: A0A1I7F002_9FLAO 
ID   A0A1I7F002_9FLAO        Unreviewed;       329 AA.
AC   A0A1I7F002;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SFU29506.1};
GN   ORFNames=SAMN05216480_101485 {ECO:0000313|EMBL:SFU29506.1};
OS   Pustulibacterium marinum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Pustulibacterium.
OX   NCBI_TaxID=1224947 {ECO:0000313|EMBL:SFU29506.1, ECO:0000313|Proteomes:UP000199138};
RN   [1] {ECO:0000313|EMBL:SFU29506.1, ECO:0000313|Proteomes:UP000199138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12333 {ECO:0000313|EMBL:SFU29506.1,
RC   ECO:0000313|Proteomes:UP000199138};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S66 family.
CC       {ECO:0000256|ARBA:ARBA00010233}.
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DR   EMBL; FPBK01000001; SFU29506.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I7F002; -.
DR   STRING; 1224947.SAMN05216480_101485; -.
DR   Proteomes; UP000199138; Unassembled WGS sequence.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   CDD; cd07025; Peptidase_S66; 1.
DR   Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR   Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR   InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR027478; LdcA_N.
DR   InterPro; IPR040449; Peptidase_S66_N.
DR   InterPro; IPR040921; Peptidase_S66C.
DR   InterPro; IPR003507; S66_fam.
DR   PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR   Pfam; PF02016; Peptidase_S66; 1.
DR   Pfam; PF17676; Peptidase_S66C; 1.
DR   PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW   ECO:0000313|EMBL:SFU29506.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199138};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..329
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011556344"
FT   DOMAIN          38..155
FT                   /note="LD-carboxypeptidase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02016"
FT   DOMAIN          201..317
FT                   /note="LD-carboxypeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17676"
FT   ACT_SITE        137
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        232
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT   ACT_SITE        302
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ   SEQUENCE   329 AA;  36586 MW;  B5DE89BDEA3F1475 CRC64;
     MIMKKLLATS LCYLLFSVTI LSAQSMKQPP FLKKGDTVAI VAPAGIIKSN RSYVFQAAEN
     YLKSLGLHVS VGKNVLKQGG HFAGSDEERC ADFQTALDDP SIKAIWCARG GYGSVRILDM
     LDYTKFKKHP KWIIGYSDIT AFHNQMNVLG YQSLHAMMCT SLESDATQIK ETKSTFEKAI
     FGQELTYSIP SNSHNYHGNA TGQLVGGNLS LLVSMLGSKT ALDTSGKIVF IEEIGEYKYS
     IDRMMQSLKR AGFFDNCKGI VFGDITRIKN NPTKFGKIIY ELLLDVVTEY NVPILFDFPA
     GHEPDNRALF LGRNVELKVN DQKSTLKFL
//
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