ID D4L1C8_9FIRM Unreviewed; 299 AA.
AC D4L1C8;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:CBL13418.1};
GN ORFNames=RO1_30730 {ECO:0000313|EMBL:CBL13418.1};
OS Roseburia intestinalis XB6B4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Roseburia.
OX NCBI_TaxID=718255 {ECO:0000313|EMBL:CBL13418.1, ECO:0000313|Proteomes:UP000008953};
RN [1] {ECO:0000313|EMBL:CBL13418.1, ECO:0000313|Proteomes:UP000008953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB6B4 {ECO:0000313|EMBL:CBL13418.1,
RC ECO:0000313|Proteomes:UP000008953};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Bernalier A.;
RT "The genome sequence of Roseburia intestinalis XB6B4.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL13418.1, ECO:0000313|Proteomes:UP000008953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XB6B4 {ECO:0000313|EMBL:CBL13418.1,
RC ECO:0000313|Proteomes:UP000008953};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929050; CBL13418.1; -; Genomic_DNA.
DR AlphaFoldDB; D4L1C8; -.
DR KEGG; rix:RO1_30730; -.
DR PATRIC; fig|718255.3.peg.400; -.
DR HOGENOM; CLU_027070_7_0_9; -.
DR Proteomes; UP000008953; 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:SF34; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACC; 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:CBL13418.1};
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:CBL13418.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 21..254
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 53
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 56
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 109
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 224
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 299 AA; 33514 MW; DD649FEBD4306047 CRC64;
MILLTGSMCI PVYAAEYWPE GPEVVSPNVI VMEASTGTVL YDCDSLEAHY PASITKIMTT
LIALENSDLN DIVTFSDAAI DNTEGSGIAR DYGEQMTMEQ CLYAVMLASA NECAYAVAEH
VGGTIENFVA MMNEKAKELG CQNTHFANPH GLHDENHYTC CYDMALIARA AYQNETFRII
VGTARYTIPP TNKHAEQTDL QNHNEMLYPF QTNKYVYDGC TGGKTGYTNA ANSTLVTYAE
RDGMTLICVV MNTQSPNQWL DSRNLFDYCF DNFQLFNIAE NETNYTSAEQ KKRRYTQYK
//
