ID A0A1F6I7B2_9BACT Unreviewed; 303 AA.
AC A0A1F6I7B2;
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=A2868_02330 {ECO:0000313|EMBL:OGH18579.1};
OS Candidatus Levybacteria bacterium RIFCSPHIGHO2_01_FULL_40_15b.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798594 {ECO:0000313|EMBL:OGH18579.1, ECO:0000313|Proteomes:UP000176941};
RN [1] {ECO:0000313|EMBL:OGH18579.1, ECO:0000313|Proteomes:UP000176941}
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:OGH18579.1}.
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DR EMBL; MFNR01000021; OGH18579.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6I7B2; -.
DR Proteomes; UP000176941; 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 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 74..276
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 303 AA; 34083 MW; 26A206EAD175A67C CRC64;
MLRLKDLLII IIGAVIFSLA LFFFFPVKQK FQEIISPLAA GLEETKNLLA GFTGNSLKET
VDSSLKGTHG TYAVIIKNLR TGEYFSQNEK RTYEPASLYK LWVLGAAFKQ IKEGKLNRDE
IISRDARDLN EIFDIASDSA ELTEGTVTMK ISDAIEQMIT ISHNYAALLL VSKIRNSNVS
AFMREQGFSS SRLGQPPRTT AEDIASFFEK LYTGAMVDGE YSKRMLDLLS QQRLNDRIPK
YLPDDVEVAH KTGEIRGFKH DAGIIFAKDP ILLVVLSESN SQQGAAERIA QLSKNVYYYF
ERK
//
