ID A0A0G0MGK7_9BACT Unreviewed; 307 AA.
AC A0A0G0MGK7;
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=UT26_C0008G0020 {ECO:0000313|EMBL:KKR03159.1};
OS Microgenomates group bacterium GW2011_GWC1_39_12.
OC Bacteria.
OX NCBI_TaxID=1618514 {ECO:0000313|EMBL:KKR03159.1, ECO:0000313|Proteomes:UP000034167};
RN [1] {ECO:0000313|EMBL:KKR03159.1, ECO:0000313|Proteomes:UP000034167}
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:KKR03159.1}.
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DR EMBL; LBWD01000008; KKR03159.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MGK7; -.
DR Proteomes; UP000034167; 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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 80..282
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 307 AA; 34899 MW; B13104087DF72C84 CRC64;
MSKKRTSIGR FIIFLFFLTL LIIVLYQTFR LIKKEPIISP IPPNEKVAVN IFSFLSKKKD
PDELKKLIKQ KIGLDWKNYS ILVVDTKSDF RVAINDTEMF TAASVNKIPI LAALYIGIQN
TDIDPDTVIT VQEEDIQDYG TGSIRYDGAG STYTIKTLAR LMMQQSDNTA AYILANHIIR
LDTIQSLLNE WGMTQTDMIN NKTANNDVYK IIKKIYQGNI ANPAYTQEML AFFKDTEFED
RIPGLLPKTV QVYHKIGSEI GYMHDVGVVV APSITYYIGI FTSDITNEKE ATKLMAEVSK
LVYDYIK
//
