ID A0QV34_MYCS2 Unreviewed; 275 AA.
AC A0QV34;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 121.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:ABK73743.1};
GN OrderedLocusNames=MSMEG_2432 {ECO:0000313|EMBL:ABK73743.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK73743.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK73743.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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DR EMBL; CP000480; ABK73743.1; -; Genomic_DNA.
DR RefSeq; WP_011728339.1; NZ_SIJM01000012.1.
DR RefSeq; YP_886772.1; NC_008596.1.
DR AlphaFoldDB; A0QV34; -.
DR STRING; 246196.MSMEG_2432; -.
DR MEROPS; S11.011; -.
DR PaxDb; 246196-MSMEI_2371; -.
DR GeneID; 66733846; -.
DR KEGG; msm:MSMEG_2432; -.
DR PATRIC; fig|246196.19.peg.2397; -.
DR eggNOG; COG1686; Bacteria.
DR OrthoDB; 3663940at2; -.
DR BRENDA; 3.4.17.8; 3512.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR018044; Peptidase_S11.
DR InterPro; IPR001967; Peptidase_S11_N.
DR PANTHER; PTHR21581; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR21581:SF33; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB1; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:ABK73743.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:ABK73743.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..275
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010197472"
FT DOMAIN 41..255
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 71
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 74
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 228
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 275 AA; 29027 MW; F16887AEA7C6A68E CRC64;
MRRLFAAAAF ALSTALAAAT FTPVAHAEPA AAPAGAAAVT DGPAKAWLVA DMDTGRVLAS
KDPYGSYAPA STIKPLLAMV VLDHLRPDNF ARANASHTKV ECSCVGLKPG QPYTTRQLLD
ALLMVSGNDA ANMLADMLGG PRVAVAAMNR KAAAVGARNT RAASPSGLDG PGWESLTTPH
DLAVIFRAAL NYPVIAQILR QTTAQFPGKT LTYQNELLTR YPGDIGGKTG YTNLARKTYV
GAAQRGNRRL VVVQMYGTGD LYDQAIRLFD YGFSQ
//
