ID A0A1C7GT44_9FIRM Unreviewed; 338 AA.
AC A0A1C7GT44;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:ANU55515.1};
GN ORFNames=A4V00_16695 {ECO:0000313|EMBL:ANU55515.1};
OS Hungateiclostridiaceae bacterium KB18.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae.
OX NCBI_TaxID=1834198 {ECO:0000313|EMBL:ANU55515.1, ECO:0000313|Proteomes:UP000092525};
RN [1] {ECO:0000313|Proteomes:UP000092525}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KB18 {ECO:0000313|Proteomes:UP000092525};
RA Uchimura Y., Wyss M., Brugiroux S., Limenitakis J.P., Stecher B.,
RA McCoy K.D., Macpherson A.J.;
RT "Complete Genome Sequences of Twelve Strains of a Stable Defined Moderately
RT Diverse Mouse Microbiota 2 (sDMDMm2).";
RL Submitted (APR-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; CP015400; ANU55515.1; -; Genomic_DNA.
DR RefSeq; WP_066540604.1; NZ_CP021422.1.
DR AlphaFoldDB; A0A1C7GT44; -.
DR STRING; 1834198.A4V00_16695; -.
DR GeneID; 83336040; -.
DR KEGG; ruk:A4V00_16695; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000092525; Chromosome.
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:ANU55515.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:ANU55515.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000092525}.
FT DOMAIN 16..137
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 208..323
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
SQ SEQUENCE 338 AA; 37575 MW; E3139FE50213A56F CRC64;
MKELIKPQRI HPGDTVATIS ISGGRAGDKD MLWRYELGKR RLQEVFGLKV VETPHALAGN
EYIYQHPELR AADLHWALEN PEVKAIITNM GGDDSYRLFP YLDYGLIRSH PKIFMGFSDI
TTSCCIFAHA GVMSYYGPSL LTPIAQPGRL DEYTESAMRK ALFSGEIIGR VEPCPKYTPI
EWQDKPEEDI VWQENPGYKL IQGRGKVQGR LIGGCWGPLQ QIMGTNIFPD RELWEGSIIF
MENISPYNSA LAALHGWRAL AASGALDVCA GIITPAMSEK EDQMLLKVLR QEVHREDLPV
LEGVDFGHRT PMTVLPIGAL AELDCASASF TILESGVC
//
