ID M1MT68_9CLOT Unreviewed; 289 AA.
AC M1MT68;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:AGF57916.1};
GN ORFNames=Cspa_c41630 {ECO:0000313|EMBL:AGF57916.1};
OS Clostridium saccharoperbutylacetonicum N1-4(HMT).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=931276 {ECO:0000313|EMBL:AGF57916.1, ECO:0000313|Proteomes:UP000011728};
RN [1] {ECO:0000313|EMBL:AGF57916.1, ECO:0000313|Proteomes:UP000011728}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N1-4(HMT) {ECO:0000313|Proteomes:UP000011728};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium saccharoperbutylacetonicum N1-4(HMT).";
RL Submitted (FEB-2013) 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; CP004121; AGF57916.1; -; Genomic_DNA.
DR RefSeq; WP_015394227.1; NZ_AOIF01000038.1.
DR AlphaFoldDB; M1MT68; -.
DR STRING; 36745.CLSAP_39150; -.
DR KEGG; csr:Cspa_c41630; -.
DR PATRIC; fig|931276.5.peg.4194; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_1_1_9; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000011728; 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:SF5; CARBOXYPEPTIDASE YOCD-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:AGF57916.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000313|EMBL:AGF57916.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011728}.
FT DOMAIN 10..127
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 171..285
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 109
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 202
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 270
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 289 AA; 32731 MW; 82EC13CAADF86711 CRC64;
MKLLSSGDKV GIVACSNGLD EKNRNKILNL ENVLGTFGLN LVYSERIYKS YSVFNGNGRE
RAEAVMKFFL DEEIKAIFDV SGGDVANEVL EYLDFEVIKK NPKPFFGYSD LSVVINALYS
KTNMKTYLYQ IRNLVESNDE RQIEEFKSTF MGEGNELLKF NYEWIQGRSM EGTIVGGNIR
CLLKLSGTEY MPDFQDKIIL FEGLGGDVPK MATYLTQYKQ LGVFKKVKGI ILGSFTEMEK
EKYSPNIVEL LKEKINDTNI PIVKTSEIGH GKESRCIIIG EKVKLFCGN
//
