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Database: UniProt
Entry: A0A0G0XI00_9BACT
LinkDB: A0A0G0XI00_9BACT
Original site: A0A0G0XI00_9BACT 
ID   A0A0G0XI00_9BACT        Unreviewed;       315 AA.
AC   A0A0G0XI00;
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=UU81_C0006G0015 {ECO:0000313|EMBL:KKS24499.1};
OS   Microgenomates group bacterium GW2011_GWC1_41_8.
OC   Bacteria.
OX   NCBI_TaxID=1618519 {ECO:0000313|EMBL:KKS24499.1, ECO:0000313|Proteomes:UP000034304};
RN   [1] {ECO:0000313|EMBL:KKS24499.1, ECO:0000313|Proteomes:UP000034304}
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:KKS24499.1}.
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DR   EMBL; LCCB01000006; KKS24499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0XI00; -.
DR   Proteomes; UP000034304; 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        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          83..285
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   315 AA;  36226 MW;  BE4F6D4B43821CF8 CRC64;
     MPRQRKISYN YKTSESIEKK SIKPVIYFLL LFFTVFVVFN MRNTTTKASN VLPFNAVSDE
     PQTLSELSLA IRNRIAEEEG TYSIRFEDFG TKNAFGINDE PVVTAASVIK IPALAALYYL
     AEQRDIDLNE VITIPESDMQ RWGTGIIRYQ DAGATYTIRE LAQVMMEHSD NTAVYVLANR
     VIGLERLQEL IDSWGLSNTN YLENNISNKD MNKVMRMMYS GELVKDEELN VEMMGWMDDS
     DFEERLPKYI PEEVSVYHKI GNEVRITHDV GVIDLPEKPY YLGVLGIEIP DHEHATEVIA
     QISQMVFEYQ SRMNQ
//
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