ID R7IX03_9FIRM Unreviewed; 344 AA.
AC R7IX03;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=LD-carboxypeptidase {ECO:0000313|EMBL:CDE56159.1};
GN ORFNames=BN596_00015 {ECO:0000313|EMBL:CDE56159.1};
OS Roseburia sp. CAG:303.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=1262944 {ECO:0000313|EMBL:CDE56159.1, ECO:0000313|Proteomes:UP000018355};
RN [1] {ECO:0000313|EMBL:CDE56159.1, ECO:0000313|Proteomes:UP000018355}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:303 {ECO:0000313|Proteomes:UP000018355};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CDE56159.1}.
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DR EMBL; CBJD010000284; CDE56159.1; -; Genomic_DNA.
DR AlphaFoldDB; R7IX03; -.
DR STRING; 1262944.BN596_00015; -.
DR Proteomes; UP000018355; 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:CDE56159.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:CDE56159.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018355}.
FT DOMAIN 13..135
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 208..330
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 115
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 247
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 315
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 344 AA; 38962 MW; 6CD538F7F1157156 CRC64;
MKYGKFLEEG GTIGFVAPSF GCNIEPYRTG FEQAQKKLQV LGHKTWLGPN CYEGKGIGIS
NTPQLCGKEL QEAYLSKESD VLISCGGGEL MCEILDYVDF DRIKKADPKW YMGYSDNTNM
TFLLTTLCDT ASIYGPCAPA FGMNPWHPAI DDAYQVLTGK KRVLNGYDGW EKESLKDEEH
PTEPYHITEE KVLHTFAGAE KVIHAQMQGR LIGGCMDCLV NLTGTKYDKV NEFTEKYKED
GFIWFLESCD LNVMAIRRAV WQMKHAGWFR YVKGFLIGRP LVFGQEMMEL DQYHAVIDLL
KDYNVPVIMD VDLGHLPPMM PLICGSMAEV RNDGNHLEIE MKLI
//