ID A0A1G1WDC6_9BACT Unreviewed; 288 AA.
AC A0A1G1WDC6;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=A2Z24_00985 {ECO:0000313|EMBL:OGY25696.1};
OS Candidatus Woykebacteria bacterium RBG_16_44_10.
OC Bacteria; Candidatus Woykebacteria.
OX NCBI_TaxID=1802597 {ECO:0000313|EMBL:OGY25696.1, ECO:0000313|Proteomes:UP000177588};
RN [1] {ECO:0000313|EMBL:OGY25696.1, ECO:0000313|Proteomes:UP000177588}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC ChEBI:CHEBI:140347; EC=3.5.2.6;
CC Evidence={ECO:0000256|ARBA:ARBA00001526};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009}.
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:OGY25696.1}.
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DR EMBL; MHCT01000023; OGY25696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1WDC6; -.
DR STRING; 1802597.A2Z24_00985; -.
DR Proteomes; UP000177588; 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:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..257
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 288 AA; 32194 MW; ADAC2850DD7DE8E8 CRC64;
MRKNLLTVLI LLVIIGIIAG IVFLAWRFIQ SRNTEPPAKL PNKEDQKKER VAKQEVLLES
IKEIVATESP GTSLSLAIYD LKNNEYFGAN DTSPQHAASV SKVLTAVYVL DQVEKGKASL
ADPLGAYNVE FQLKATVNQS DPETWALLDE RFKPTDQNKF AKSVGLENTD IRIGKNLMAP
KDVAVLLKKL AKGELLKDYH RDKLFTYMQN TESENFFSPS FTQSGLTFYH KTGKFETEAH
DAAIVNHPEN PFVLVVFSVN NSNLDPNTRG PLMQKVASTV LDYFDSLD
//
