ID A0A1F8CN41_9BACT Unreviewed; 349 AA.
AC A0A1F8CN41;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN ORFNames=A2210_01350 {ECO:0000313|EMBL:OGM77128.1};
OS Candidatus Woesebacteria bacterium RIFOXYA1_FULL_40_18.
OC Bacteria; Candidatus Woesebacteria.
OX NCBI_TaxID=1802532 {ECO:0000313|EMBL:OGM77128.1, ECO:0000313|Proteomes:UP000177855};
RN [1] {ECO:0000313|EMBL:OGM77128.1, ECO:0000313|Proteomes:UP000177855}
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:OGM77128.1}.
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DR EMBL; MGHS01000007; OGM77128.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8CN41; -.
DR STRING; 1802532.A2210_01350; -.
DR Proteomes; UP000177855; 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 49..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 124..323
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 22..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 349 AA; 39651 MW; A7A7FBB27980646A CRC64;
MSIFNRKKDE DEEDLDDKKF EDKKFKDLNP QNKRKRKEPQ KPWGRPERLL VLSVLLATIF
LSAFLGLFAR DFKLPGLPRL SMPSFDFFEG ETIVIKGNKQ SEEKSKKISE EFKNITKNLS
GVYGLYVIRL NGEGAYGIFD KEKFEAASLV KLPVLATLYK EAEAGNIDLD TKYSLKNSDK
ITGSGSLSGK PAGTVLTYRD LARFMGKQSD NTAYGIIKRI LGDAKINKEI SDLGMTNTSL
SDHSTSPYDT GIFFEKLYKN QIVKEKYKNE ILDYLTDTIY ENWLVAGIPE EIRVAHKYGR
ELHVVNDAGV VFTKEPFILV IMTKGVVERE ADEFFPKLTK VIYDGETSK
//
