ID   A0A0G1WG26_9BACT        Unreviewed;       329 AA.
AC   A0A0G1WG26;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Serine-type D-Ala-D-Ala carboxypeptidase {ECO:0000313|EMBL:KKW17706.1};
GN   ORFNames=UY57_C0011G0003 {ECO:0000313|EMBL:KKW17706.1};
OS   Candidatus Kaiserbacteria bacterium GW2011_GWB1_50_17.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1618673 {ECO:0000313|EMBL:KKW17706.1, ECO:0000313|Proteomes:UP000034120};
RN   [1] {ECO:0000313|EMBL:KKW17706.1, ECO:0000313|Proteomes:UP000034120}
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   -!- 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:KKW17706.1}.
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DR   EMBL; LCQM01000011; KKW17706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1WG26; -.
DR   Proteomes; UP000034120; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000871; Beta-lactam_class-A.
DR   InterPro; IPR001967; Peptidase_S11_N.
DR   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00768; Peptidase_S11; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:KKW17706.1};
KW   Hydrolase {ECO:0000313|EMBL:KKW17706.1};
KW   Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:KKW17706.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        26..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          71..306
FT                   /note="Peptidase S11 D-alanyl-D-alanine carboxypeptidase A
FT                   N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00768"
SQ   SEQUENCE   329 AA;  35065 MW;  45E60AA1C4C589FB CRC64;
     METQKEQPGE LPDEKYQHPR PPVGNMLGAG FLAVFLFGTL AITAIYVFPL ENPESQVASA
     ASVYDPYANV KLSATSAIVV DLTNGKTLFA LNTDTQLPLA SLTKIALVQA ASEVLLPDDI
     IFVARDITSA GGVQILPAGK SWRTQDIIDA VLVASSNNGA EILAEVANKL LHERFPEAPA
     DTTLWRMNAL ARELGLKQTY FLSVNGLDVS DTFASAYGSA RDMATLFTHA FETNSMAFSG
     TAREGITFIS SDETQGTIAR NTNELAGVIP GLIMGKTGFT DLAGGNLVVI FDVGIVHPVV
     AVVLGSTQEG RFEDMQKLVN VTRTLITAE
//