ID A0A1D7XL62_9CLOT Unreviewed; 425 AA.
AC A0A1D7XL62;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase {ECO:0000313|EMBL:AOR24093.1};
GN ORFNames=BGI42_10265 {ECO:0000313|EMBL:AOR24093.1};
OS Clostridium taeniosporum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=394958 {ECO:0000313|EMBL:AOR24093.1, ECO:0000313|Proteomes:UP000094652};
RN [1] {ECO:0000313|Proteomes:UP000094652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1/k {ECO:0000313|Proteomes:UP000094652};
RA Walker J.R.;
RT "Genomics of Clostridium taeniosporum, an organism which forms endospores
RT with ribbon-like appendages.";
RL Submitted (SEP-2016) 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; CP017253; AOR24093.1; -; Genomic_DNA.
DR RefSeq; WP_069680232.1; NZ_CP017253.2.
DR AlphaFoldDB; A0A1D7XL62; -.
DR STRING; 394958.BGI42_10265; -.
DR KEGG; ctae:BGI42_10265; -.
DR OrthoDB; 1701915at2; -.
DR Proteomes; UP000094652; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:AOR24093.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:AOR24093.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000094652};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..425
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009102028"
FT TRANSMEM 389..413
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 32..263
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 68
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 71
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 130
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 425 AA; 47616 MW; 01CA8620B9925209 CRC64;
MKRNLILKTL ALTITLSLFA PFSVKSYATE NTTQSLPSIQ AESALTMDYE TGEIIYTKDA
DSKRYPASTT KLLTGLLLAE KFEKNSEITF TQSAKEQPEY SLNINYMHNR MQIGDKMLAD
NVMKGLLLFS GNDTAYMIAD NVAGSAEAFS ELMNKKAKEL GANNSNFITA NGLHDPNHYT
TAYDLSLITK AAFENPWERE TMSLKEAPID INGSRIILEN RNLGLGKNGN LGGKTGFTNA
AGGCLAAVYE KDGRKIIGVV LKSRQINNAD MTKFNDMDSI IDYSYSTNKE IYKKTNEEVG
TTDLQYKSFG FFGPTRTITV PIVLSQDVMY YKNDINDAES SITYNASNNS AWNLAFNKNT
NLTYSTRNHV EEVKGMIDIS VGKILKDNIL LYSTVLVIAI IMITLIILIR NMAKNNRKRR
YRRRY
//
