ID A0A0L6Z7Y8_9CLOT Unreviewed; 305 AA.
AC A0A0L6Z7Y8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Putative murein peptide carboxypeptidase {ECO:0000313|EMBL:KOA19086.1};
DE EC=3.4.16.- {ECO:0000313|EMBL:KOA19086.1};
GN Name=ykfA {ECO:0000313|EMBL:KOA19086.1};
GN ORFNames=CLHOM_24670 {ECO:0000313|EMBL:KOA19086.1};
OS Clostridium homopropionicum DSM 5847.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121318 {ECO:0000313|EMBL:KOA19086.1, ECO:0000313|Proteomes:UP000037043};
RN [1] {ECO:0000313|Proteomes:UP000037043}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5847 {ECO:0000313|Proteomes:UP000037043};
RA Poehlein A., Beck M., Schiel-Bengelsdorf B., Bengelsdorf F.R., Daniel R.,
RA Duerre P.;
RT "Genome sequence of the strict anaerobe Clostridium homopropionicum LuHBu1
RT (DSM 5847T).";
RL Submitted (AUG-2015) 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:KOA19086.1}.
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DR EMBL; LHUR01000028; KOA19086.1; -; Genomic_DNA.
DR RefSeq; WP_052221973.1; NZ_LHUR01000028.1.
DR AlphaFoldDB; A0A0L6Z7Y8; -.
DR STRING; 36844.SAMN04488501_1195; -.
DR PATRIC; fig|1121318.3.peg.2483; -.
DR Proteomes; UP000037043; 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:KOA19086.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KOA19086.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000037043};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 12..128
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 175..290
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 108
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 205
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 275
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 305 AA; 33852 MW; 69FAA19C7D3FE23C CRC64;
MIGKRLKKGC IIGLISPSSP ENPEKIKDSI STLRNHGFNI KEGNFLYEKR GYLAGGDKER
AQDFMNMFKD ESVDMILCMR GGYGSMRILP LIDYEIIKNN PKIFIGYSDI TALLNTISSR
CDLITFHGPM GNSNFNDIET LGSFLTTLMN GHRPYKLLNP LGINLTRNIG GKAVGKIVGG
NLSLITATLG TPYEIDTKNN ILFMEDINEQ PYVIDRMLTQ LHLSGKLEQC SGFIIGQFTG
CSLPNYEKSL TTNEVMLDRI LSLNKPTLSN FMCGHDYPNL TLPIGAKGEI DCDKGEINIL
EPVVK
//
