ID A0A1G5BK69_9FIRM Unreviewed; 279 AA.
AC A0A1G5BK69;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA (Peptidoglycan recycling) {ECO:0000313|EMBL:SCX90494.1};
GN ORFNames=SAMN02910371_00367 {ECO:0000313|EMBL:SCX90494.1};
OS Butyrivibrio sp. INlla14.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Butyrivibrio.
OX NCBI_TaxID=1520808 {ECO:0000313|EMBL:SCX90494.1, ECO:0000313|Proteomes:UP000199551};
RN [1] {ECO:0000313|Proteomes:UP000199551}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INlla14 {ECO:0000313|Proteomes:UP000199551};
RA Varghese N., Submissions S.;
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; FMVS01000003; SCX90494.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5BK69; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000199551; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR CDD; cd07062; Peptidase_S66_mccF_like; 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:SF5; CARBOXYPEPTIDASE YOCD-RELATED; 1.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE 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:0000313|EMBL:SCX90494.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:SCX90494.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199551}.
FT DOMAIN 4..119
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 164..275
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 102
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 195
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 262
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 279 AA; 31039 MW; 119151620E9238AA CRC64;
MKAGIVACSN GQRKEWKEQN EQLVDVLNIM GIEAVLSLHI MSKTDEFSGT DEERAADLMK
FWTDDSIDAI YDISGGDLAN GILKYLDYDL IAKSDKMFWG YSDLTTVINA IFAMTGKSSV
LYQIKNMVYS KSDLQQKRFS SYLSGKESEL LDFNYDFIQG NQMEGIIVGG NIRCLLKLAG
TKYWPDLNGK ILLLESLGGE SGQIATLFSQ LEQMGVFDQV AGVLLGTFTE YEKADLELSV
FDLLKMHINN TLPVASTREI GHGNDSKAII IGKNILLHK
//
