ID H1AFJ1_ENTAS Unreviewed; 270 AA.
AC H1AFJ1;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE Flags: Fragment;
GN Name=bla SHV {ECO:0000313|EMBL:BAL43175.1};
OS Enterobacter asburiae.
OG Plasmid pGM3-3 {ECO:0000313|EMBL:BAL43175.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=61645 {ECO:0000313|EMBL:BAL43175.1};
RN [1] {ECO:0000313|EMBL:BAL43175.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=GM3-3 {ECO:0000313|EMBL:BAL43175.1};
RC PLASMID=pGM3-3 {ECO:0000313|EMBL:BAL43175.1};
RA Mbehang Nguema P.P., Tsuchida S., Takahashi S., Fujita S., Yamagiwa J.,
RA Ushida K.;
RT "Isolation of enterobacteriaceae highly resistant to beta-lactam
RT antibiotics from wild gorillas in Moukalaba-Doudou National Park Gabon.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; AB675722; BAL43175.1; -; Genomic_DNA.
DR AlphaFoldDB; H1AFJ1; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
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 InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; D-ALANYL-D-ALANINE ENDOPEPTIDASE; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Plasmid {ECO:0000313|EMBL:BAL43175.1}.
FT DOMAIN 26..239
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 251..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAL43175.1"
FT NON_TER 270
FT /evidence="ECO:0000313|EMBL:BAL43175.1"
SQ SEQUENCE 270 AA; 29437 MW; EA6C5B760AC722B2 CRC64;
VQQPQPLEQI KLSESQLSGR VGMIEMDLAS GRTLTAWRAD ERFPMMSTFK VVLCGAVLAR
VDAGDEQLER KIHYRQQDLV DYSPVSEKHL ADGMTVRELC AAAITMSDNS AANLLLATVG
GPAGLTAFLR QIGDNVTRLD RWETELNEAL PGDARDTTTP ASMAATLRKL LTSQRLSARS
QRQLLQWMVD DRVAGPLIRS VLPAGWFIAD KTGAGERGAR GIVALLGPNN KAERIVVILS
CGIRPASMAE RNQQIAGDRR GANQKGKTYN
//