ID A0A173XGM0_9CLOT Unreviewed; 322 AA.
AC A0A173XGM0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Peptidase S11 D-alanyl-D-alanine carboxypeptidase 1 {ECO:0000313|EMBL:CUN51012.1};
DE EC=3.4.16.4 {ECO:0000313|EMBL:CUN51012.1};
GN Name=dacB_1 {ECO:0000313|EMBL:CUN51012.1};
GN ORFNames=ERS852407_00411 {ECO:0000313|EMBL:CUN51012.1};
OS Hungatella hathewayi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX NCBI_TaxID=154046 {ECO:0000313|EMBL:CUN51012.1, ECO:0000313|Proteomes:UP000095651};
RN [1] {ECO:0000313|EMBL:CUN51012.1, ECO:0000313|Proteomes:UP000095651}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2789STDY5608850 {ECO:0000313|EMBL:CUN51012.1,
RC ECO:0000313|Proteomes:UP000095651};
RG Pathogen Informatics;
RL Submitted (SEP-2015) 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; CYZE01000001; CUN51012.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A173XGM0; -.
DR Proteomes; UP000095651; Unassembled WGS sequence.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
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:SF32; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB; 1.
DR Pfam; PF00768; Peptidase_S11; 1.
DR PRINTS; PR00725; DADACBPTASE1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:CUN51012.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CUN51012.1};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:CUN51012.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000095651};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 67..304
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 100
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 103
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 157
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 273
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 322 AA; 34715 MW; 8F719ED3E81A87C0 CRC64;
MKKKITMKAG CAFLCVTMLS GCSSFKKLDN PYDFAQRTAL YEGTTLSDRA ESFAHNLCVV
TADTPSTDQA VTAEAAAVFD LSDKTVIFGK NPFEKLYPAS ITKTMTALLA IKYGNLSDEV
TVPEEAVITE SGATLCGIKP GDKLTMEQLL YGLMLPSGND AGAAIAVHMD GSIEKFADRM
NEEARKLGAT GTHFVNPHGL NDENHYTTAY DLYLIFNEAM KYPDFRKVIG TSSYDAVYAS
ASGDTLTKTW KQSNWYMTGE RDMPEGLTAL GGKTGTTKAA GSCLIMGSSG SSGMEYISVV
LKAPDRTGLY DNMSNILNKI VD
//
