ID A0A0G0NKD8_9BACT Unreviewed; 302 AA.
AC A0A0G0NKD8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KKQ77566.1};
GN ORFNames=US99_C0038G0008 {ECO:0000313|EMBL:KKQ77566.1};
OS Candidatus Daviesbacteria bacterium GW2011_GWF2_38_6.
OC Bacteria; Candidatus Daviesbacteria.
OX NCBI_TaxID=1618432 {ECO:0000313|EMBL:KKQ77566.1, ECO:0000313|Proteomes:UP000034324};
RN [1] {ECO:0000313|EMBL:KKQ77566.1, ECO:0000313|Proteomes:UP000034324}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKQ77566.1}.
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DR EMBL; LBVC01000038; KKQ77566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0NKD8; -.
DR PATRIC; fig|1618432.3.peg.532; -.
DR Proteomes; UP000034324; 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:KKQ77566.1};
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:KKQ77566.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 56..285
FT /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00768"
FT ACT_SITE 90
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT ACT_SITE 145
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-1"
FT BINDING 255
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR618044-2"
SQ SEQUENCE 302 AA; 33406 MW; E5128C24B6B977A6 CRC64;
MKKLAALLFI FIFLLLVLLS SSLSKGEINL ISPISVQEKV LGINQWFPGN INAVQLDAPK
VTAEAALFID TKTGQVFYSK NPNKKLPIAS LVKVMTVLIA LEHKNMDDQF TVSQYAADME
PDKMLLIAGE KLTLKELLYG IFLISANDAA EVLSEGTTGD KDEFIKLMNI KAKQVGMNDS
LFVNPTGLDE DSNNSYSSAY DLAILSRYLI KHYPEIVEIS RTPYIYLPVT ENHQDYDMYS
GINLLTTYPG VVGLKTGYTP EAGLTLITLA RKESREVLGV LLGSQARRDE ARNLLNFSLS
AI
//
