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Database: UniProt
Entry: A0A0G0I6A9_9BACT
LinkDB: A0A0G0I6A9_9BACT
Original site: A0A0G0I6A9_9BACT 
ID   A0A0G0I6A9_9BACT        Unreviewed;       315 AA.
AC   A0A0G0I6A9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=beta-lactamase {ECO:0000256|ARBA:ARBA00012865};
DE            EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865};
GN   ORFNames=US68_C0001G0067 {ECO:0000313|EMBL:KKQ50868.1};
OS   Candidatus Shapirobacteria bacterium GW2011_GWE1_38_10.
OC   Bacteria; Candidatus Shapirobacteria.
OX   NCBI_TaxID=1618488 {ECO:0000313|EMBL:KKQ50868.1, ECO:0000313|Proteomes:UP000034231};
RN   [1] {ECO:0000313|EMBL:KKQ50868.1, ECO:0000313|Proteomes:UP000034231}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKQ50868.1}.
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DR   EMBL; LBTX01000001; KKQ50868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0I6A9; -.
DR   PATRIC; fig|1618488.3.peg.69; -.
DR   Proteomes; UP000034231; 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..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..290
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   315 AA;  35723 MW;  CB76ED1C2B95E96B CRC64;
     MNIIKTFILL TLGLIILIFG FFLGQNRLST TLPAFTESRH QGNYQFINPL LECESTNFSQ
     NVALDSLKDQ ITKTINQLKS SGLVSFASIY YRDLNEGPWV GINEKENFSP ASLIKVPLMI
     TYYKQAESNP DVLKQTLTYL PAKDELVQDI LPSITLTSNQ EYTIEDLIRS MIVYSDNQAY
     ELLLNNIDNQ LVVETYQNLG VNIISVKSYA AFFRILFNAS YLNHEMSEKA LSLLSQVQYQ
     DGLVKGVNNP LLKIAHKFGE RTFTDTGEKQ LHDCGIVYIP QKPYLICVMT RGNDFSKLSS
     SIAQISKVIY QQQSH
//
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