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
//