ID A0A267TIG3_9BACT Unreviewed; 303 AA.
AC A0A267TIG3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:PAC32573.1};
GN ORFNames=BWI92_05070 {ECO:0000313|EMBL:PAC32573.1};
OS Flectobacillus sp. BAB-3569.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Flectobacillus.
OX NCBI_TaxID=1509483 {ECO:0000313|EMBL:PAC32573.1, ECO:0000313|Proteomes:UP000215844};
RN [1] {ECO:0000313|EMBL:PAC32573.1, ECO:0000313|Proteomes:UP000215844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAB-3569 {ECO:0000313|EMBL:PAC32573.1,
RC ECO:0000313|Proteomes:UP000215844};
RA Dhebar S., Dhebar S., Bhargava P., Bagatharia S.B., Soni S., Joshi M.N.;
RT "Flectobacillus sp. BAB-3569 genome sequencing.";
RL Submitted (JUN-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:PAC32573.1}.
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DR EMBL; NJFZ01000005; PAC32573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267TIG3; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000215844; 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:PAC32573.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000215844};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 13..129
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 172..288
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 203
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 273
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 303 AA; 33821 MW; 0A54AEEBB7719F4F CRC64;
MQKPPFLKKG DTVGVLALAW KVAFEDLEAA IAFMETEWEL KVVLGESLKT SYHQYAATDE
IRARDFQQML DNPSIKAIFS ARGGYGSARI LDQINFDAFL ENPKWLIGFS DITAVLCHAF
CLGVESIHGV MPKLFLQEGG AQSLESLKDL LFGKPISYQV PSHPMNRKGK AQGQLVGGNL
ALMVHLIGSR SEVNLSGKIL FLEDVGEYHY ALDRMMIQLK RTGQLAELAG LIVGHFSNLS
DDPSIYGKTA YEIVEEAVAE YEYPRCYGFP VGHEPENWAM PVGREMKLTV LENLCMLEER
IIE
//
