ID A0A1I0M5R2_9FIRM Unreviewed; 360 AA.
AC A0A1I0M5R2;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=D-alanyl-D-alanine carboxypeptidase (Penicillin-binding protein 5/6) {ECO:0000313|EMBL:SEV83815.1};
GN ORFNames=SAMN05421659_101229 {ECO:0000313|EMBL:SEV83815.1};
OS [Clostridium] fimetarium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=99656 {ECO:0000313|EMBL:SEV83815.1, ECO:0000313|Proteomes:UP000199701};
RN [1] {ECO:0000313|EMBL:SEV83815.1, ECO:0000313|Proteomes:UP000199701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 9179 {ECO:0000313|EMBL:SEV83815.1,
RC ECO:0000313|Proteomes:UP000199701};
RA de Groot N.N.;
RL Submitted (OCT-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; FOJI01000001; SEV83815.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0M5R2; -.
DR STRING; 99656.SAMN05421659_101229; -.
DR OrthoDB; 9791132at2; -.
DR Proteomes; UP000199701; Unassembled WGS sequence.
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:SEV83815.1};
KW Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW Protease {ECO:0000313|EMBL:SEV83815.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199701};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 32..50
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 105..335
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT COILED 2..29
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 136
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 139
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 196
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 309
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 360 AA; 39941 MW; 18E917E5951F6AE3 CRC64;
MYNNIDNSNK EATESYRRIK EKRAKQQRKM KIIKLSACII LILAVVTVVV KGTTSSNTDN
IEIENIVAVD DGNVQREVVT EPQPQGKKVY PYPEIINSYM QITSATVRSP YLALLDVENN
QIIAGRDCER RIYPASMTKV MTLIVAVEKL KRLDTTFTMT SDIVSSLMKQ QASRAGFDPG
EIVDANNLLY GLILPSGADA AVALADMIAG SEEEFVNLMN SKCEELGLKN THFVNTSGLQ
DINHYTTPIE MAMIMDYAMK NEICAKILST YQYTTTPTVQ HPEGILLTSN MFSKMYGNEV
QGMRIIAGKT GYTDQSGNCL VSYAEKNGRH YVVVIAGGGS AWNVIFDDFD IFKNYTPVIG
//
