ID A0A1M6TTX9_9FIRM Unreviewed; 335 AA.
AC A0A1M6TTX9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase LdcA (Peptidoglycan recycling) {ECO:0000313|EMBL:SHK60374.1};
GN ORFNames=SAMN02745136_02873 {ECO:0000313|EMBL:SHK60374.1};
OS Anaerocolumna jejuensis DSM 15929.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1121322 {ECO:0000313|EMBL:SHK60374.1, ECO:0000313|Proteomes:UP000184386};
RN [1] {ECO:0000313|EMBL:SHK60374.1, ECO:0000313|Proteomes:UP000184386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15929 {ECO:0000313|EMBL:SHK60374.1,
RC ECO:0000313|Proteomes:UP000184386};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FRAC01000014; SHK60374.1; -; Genomic_DNA.
DR RefSeq; WP_073277094.1; NZ_FRAC01000014.1.
DR AlphaFoldDB; A0A1M6TTX9; -.
DR STRING; 1121322.SAMN02745136_02873; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000184386; 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:SF4; CARBOXYPEPTIDASE-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:SHK60374.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:SHK60374.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184386}.
FT DOMAIN 13..133
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 202..318
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 113
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 241
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 306
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 335 AA; 37587 MW; EB118A2B8FF6D40A CRC64;
MIYPEFLTKN SLIGVAAPSE GNQKETDFNR LDNAIASLKS RGYQVIEGPL VRKSDKGRSG
SGKDRGEELN KLLEKKEVRW IVGAKGGDFL VEMLPYFDFE AISRHPVWYQ GFSDNTGLTY
TITTHCDIAT IYGSNFNDFG MSEWHPALEN NLKILSGENI TQDSFDLYED GYYDRITGLE
GYVLTQPVNL KQAAGKEGIP VEGRLLGGCL DVLLNLCGTR FDCTRSFIEK YKEEGILWYL
ESFALGSDSL IRGLWQLKEA GWFQYAKGFI FGRPAFYEEN YGISYEEAVM SVLKDVPIIL
NADIGHKAPS ITVVNGSKGS FVCKEGRGRL VMEYR
//
