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Database: UniProt
Entry: A0A1F7WZ86_9BACT
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ID   A0A1F7WZ86_9BACT        Unreviewed;       345 AA.
AC   A0A1F7WZ86;
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=A2Z67_05425 {ECO:0000313|EMBL:OGM08047.1};
OS   Candidatus Woesebacteria bacterium RBG_13_36_22.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1802478 {ECO:0000313|EMBL:OGM08047.1, ECO:0000313|Proteomes:UP000176939};
RN   [1] {ECO:0000313|EMBL:OGM08047.1, ECO:0000313|Proteomes:UP000176939}
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:OGM08047.1}.
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DR   EMBL; MGFQ01000058; OGM08047.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7WZ86; -.
DR   Proteomes; UP000176939; 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        41..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          121..320
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   345 AA;  38355 MW;  3153963900E5C965 CRC64;
     MIFSKEKEEE VITRKIQRPK EEFVKRRKKE PPKPWGKKER FLILFILLFT ILTSIVLALS
     ARAWKLPGLP RIKFPAISIF QNETIVLEND NKTASQDIID RSQKVTSDFK KNTNNLSGVY
     GLLVIDLKSG YSFGLSQGES FTAASLIKLP VMAAAFRESE KGNLNLATIY TLKDADKIAG
     SGSLYYKPAG TKLSYRELLM LMGKQSDNTA FGIMRKVLGD AKINEVIKTI GMNSTSLEDN
     STSPDDIGTF FKKLWEGKVT SKDSADEILN NLTETSFENW IVAGIPANVR VAHKYGRELH
     VVNDAGIIYA DNPFVLVILT KGVVEKEADG IFSSLAGLVY DGLEK
//
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