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Database: UniProt
Entry: A0A1F6BDF6_9BACT
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ID   A0A1F6BDF6_9BACT        Unreviewed;       313 AA.
AC   A0A1F6BDF6;
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=A2363_01775 {ECO:0000313|EMBL:OGG34930.1};
OS   Candidatus Gottesmanbacteria bacterium RIFOXYB1_FULL_47_11.
OC   Bacteria; Candidatus Gottesmanbacteria.
OX   NCBI_TaxID=1798401 {ECO:0000313|EMBL:OGG34930.1, ECO:0000313|Proteomes:UP000176186};
RN   [1] {ECO:0000313|EMBL:OGG34930.1, ECO:0000313|Proteomes:UP000176186}
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:OGG34930.1}.
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DR   EMBL; MFKE01000019; OGG34930.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6BDF6; -.
DR   STRING; 1798401.A2363_01775; -.
DR   Proteomes; UP000176186; Unassembled WGS sequence.
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}.
FT   DOMAIN          79..286
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   313 AA;  34704 MW;  095423663F7BD1E9 CRC64;
     MKSVRILLIS GVALVGLYLL LNQLVKLERA NSHVISPLTD ATVTTSTVIP PVKDRSQANS
     ERLKDVVDGA LEGATGSYGI YIKNLKTGES YVSGEHNVFD SASLYKLWVM AVVYQKIQDE
     QFTEDQVLRE DVFVLNQKFD IDPELAEKTE GVITFSVREA LRQMITVSDN YAALLLTEKI
     GLSSVATFLK ENDLTESAVG TTGGPPTSTP YDIERFLEKL YREDVANPKY TAEMIDLLKN
     QKLNNGIPKY LPDASSVANK TGEIDRFKHD AGIIYTDNGD YSIVVMSESA YPPGAQERIA
     RVSKAVFDYF THK
//
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