ID A0A1G2DGB5_9BACT Unreviewed; 322 AA.
AC A0A1G2DGB5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=A3D67_04395 {ECO:0000313|EMBL:OGZ12616.1};
OS Candidatus Lloydbacteria bacterium RIFCSPHIGHO2_02_FULL_51_22.
OC Bacteria; Candidatus Lloydbacteria.
OX NCBI_TaxID=1798663 {ECO:0000313|EMBL:OGZ12616.1, ECO:0000313|Proteomes:UP000178099};
RN [1] {ECO:0000313|EMBL:OGZ12616.1, ECO:0000313|Proteomes:UP000178099}
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:OGZ12616.1}.
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DR EMBL; MHLN01000003; OGZ12616.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2DGB5; -.
DR Proteomes; UP000178099; 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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..288
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 322 AA; 36787 MW; 67199A03CF572F41 CRC64;
MKKTEVQRNI PAYLIAAVCL LALMNATTII WYESRSVPVE NASTQYPFID KARHFISQEH
YLANFQLLRD ELSAIVEREK DGGVELSLYF EYLNTGSNIS LNQNTRLFPA SLNKLPIAMA
VTKKIENGIW RFDDKLVLLP ADINKFYGDL YKEPVGSAFT IEFLLQKILR QSDNTAFSIV
YRNLEVDEAD SALDDLGLRE LFDETGQITA KEYSRIFRAL YTASFLTREH SQTLLQWLTE
SDFNDFLARG VPADIPFAHK FGINTDQRIF ADSGIVYVPN RPYLLTVVVH PTELRTPDDD
HREAGRIMGD ISAAVFAYIH ER
//
