ID A0A1M5WJF2_9CLOT Unreviewed; 308 AA.
AC A0A1M5WJF2;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Muramoyltetrapeptide carboxypeptidase {ECO:0000313|EMBL:SHH87602.1};
GN ORFNames=SAMN02745196_01680 {ECO:0000313|EMBL:SHH87602.1};
OS Clostridium collagenovorans DSM 3089.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121306 {ECO:0000313|EMBL:SHH87602.1, ECO:0000313|Proteomes:UP000184526};
RN [1] {ECO:0000313|EMBL:SHH87602.1, ECO:0000313|Proteomes:UP000184526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3089 {ECO:0000313|EMBL:SHH87602.1,
RC ECO:0000313|Proteomes:UP000184526};
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; FQXP01000006; SHH87602.1; -; Genomic_DNA.
DR RefSeq; WP_072831584.1; NZ_FQXP01000006.1.
DR AlphaFoldDB; A0A1M5WJF2; -.
DR STRING; 1121306.SAMN02745196_01680; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000184526; 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:SHH87602.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000184526};
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 175..289
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 206
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 308 AA; 34511 MW; CA1EFA4998D73CAE CRC64;
MQQGKKLKKG DTIGLISPAG PEDPKAIRKG IEFLKSLGFN VKEGKHLYDK EKYLAGSDID
RAKDLMNMFK DKDVNMVLCV RGGYGTMRIL PLLDFDIIKK NPKIFMGFSD ITTLLNMIAQ
KSNIITFHGP MGSSSLDEKY TLESFLNILT QCRGDFTIDN PKDFDIKEEV SGYAEGEIIG
GNLCLICSTL GTPYEIDFKN KILFIEEIGE APYKIDRMLT QLLLSNKLQE CSGFILGQFK
GCQLSNYERS FKLDEVISDR ILSLGKPTLS NLMSGHDYPK LTIPIGCKCL LDTYNKSIKI
IEPVVSEN
//
