ID A0A1Y2R6V4_9BURK Unreviewed; 302 AA.
AC A0A1Y2R6V4;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:OSZ75370.1};
GN ORFNames=CAP37_08105 {ECO:0000313|EMBL:OSZ75370.1};
OS Hydrogenophaga sp. IBVHS1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1985169 {ECO:0000313|EMBL:OSZ75370.1, ECO:0000313|Proteomes:UP000194358};
RN [1] {ECO:0000313|EMBL:OSZ75370.1, ECO:0000313|Proteomes:UP000194358}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBVHS1 {ECO:0000313|EMBL:OSZ75370.1,
RC ECO:0000313|Proteomes:UP000194358};
RA Orr R.J.;
RT "Draft genome sequences of novel bacteria, isolated from environmental
RT samples.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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:OSZ75370.1}.
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DR EMBL; NFUU01000001; OSZ75370.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2R6V4; -.
DR STRING; 1985169.CAP37_08105; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000194358; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; 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:OSZ75370.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000194358};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 4..123
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 175..290
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 103
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 204
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 302 AA; 32462 MW; 593772670BF4DF6D CRC64;
MSHIYVYSPS SAVRDKAAFR RGVARLKKLG HEVELDEAAL KSHMRFAGDD ETRLAAIGRA
AASGADVALI SRGGYGLTRI LGALPVKQIT KSIERGTQFV GLSDFTALQM ALLAKTGGVT
WAGPALGEDF GAEAPDDIME ACFDDLLVGH GEGAGWTLPA GDALKESVLR VRGATLWGGN
LNVICSLVGT PYLPKIKGGI LFLEDTNEHP YRVERQLTQL LNAGVLGGQK AVLLGSFNRF
KLVPGYDRGF NMKSVVAWLR TQTKTPVFTG LPFGHVQTKV LLPVGRKVDL MVEGRDALIY
WG
//
