ID B5CLY0_9FIRM Unreviewed; 339 AA.
AC B5CLY0;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:EDY33698.1};
GN ORFNames=RUMLAC_00454 {ECO:0000313|EMBL:EDY33698.1};
OS [Ruminococcus] lactaris ATCC 29176.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Mediterraneibacter.
OX NCBI_TaxID=471875 {ECO:0000313|EMBL:EDY33698.1, ECO:0000313|Proteomes:UP000003254};
RN [1] {ECO:0000313|EMBL:EDY33698.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33698.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Ruminococcus lactaris ATCC 29176.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EDY33698.1, ECO:0000313|Proteomes:UP000003254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29176 {ECO:0000313|EMBL:EDY33698.1,
RC ECO:0000313|Proteomes:UP000003254};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S11 family.
CC {ECO:0000256|ARBA:ARBA00007164, ECO:0000256|RuleBase:RU004016}.
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:EDY33698.1}.
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DR EMBL; ABOU02000017; EDY33698.1; -; Genomic_DNA.
DR RefSeq; WP_005610062.1; NZ_DS990181.1.
DR AlphaFoldDB; B5CLY0; -.
DR MEROPS; S11.004; -.
DR GeneID; 77333918; -.
DR eggNOG; COG1686; Bacteria.
DR HOGENOM; CLU_027070_2_2_9; -.
DR Proteomes; UP000003254; Unassembled WGS sequence.
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:EDY33698.1};
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:EDY33698.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003254};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 108..318
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 114
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 171
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 287
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 339 AA; 37255 MW; 8504C564E35E7074 CRC64;
MSRRRRRRRK RRNPAGRLIA LVLTLVVAGG AAAGGIWYYA EHSGNPLTEY ADEKYNADLY
RAEPFSETLC VSAENVALDG FTDEPSLHAA GLFNLNERSV EYGYRLYDKL YPASTTKLMT
AYLALKYGKL EDMVTVTDSV TGFAIDEVVC GLYPGGQVKL YDLLCGLLLK SGNDCGVAIA
EYISGSVEAF AELMNEEAKE LGATGTHFVN PHGLHEDDHY TTAYDLYLIF NACIQNDTFK
EIISMSSYTM SIGDAAGNTH SLEVLPTNYY SLGKTEAPEG IKVFGGKTGT TDQAGCCVIL
YSEDMEAHPY ISVIMGAEDK AFLYQEMNRL LEAEKALSE
//
