ID B5WXV7_BACT4 Unreviewed; 306 AA.
AC B5WXV7;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 37.
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=cfxA {ECO:0000313|EMBL:CAP78900.1};
OS Bacteroides thetaiotaomicron.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=818 {ECO:0000313|EMBL:CAP78900.1};
RN [1] {ECO:0000313|EMBL:CAP78900.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MN17 {ECO:0000313|EMBL:CAP78900.1};
RA Garcia N., Gutierrez G., Lorenzo M., Garcia J.E., Piriz S., Quesada A.;
RT "Genetic determinants for cfxA expression in Bacteroides strains isolated
RT from human infections.";
RL J. Antimicrob. Chemother. 62:942-947(2008).
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; AM940017; CAP78900.1; -; Genomic_DNA.
DR AlphaFoldDB; B5WXV7; -.
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; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
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}.
FT DOMAIN 51..274
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAP78900.1"
SQ SEQUENCE 306 AA; 33684 MW; B7EA12A59F6FC877 CRC64;
LVCIFILVFS LFHKSATKDS ANPPLTNVLT DSISQIVSAC PCEIGVAVIV NNRDTVKVNN
KSVYPMMSVF KVHQALALCN DFDNKGISLD TLVNINRDKL DPKTWSPMLK DYSGPVISLT
VRDLLRYTLT QSDNNASNLM FKDMVNVAQT DSFIATLIPR SSFQIAYTEE EMSADHNKAY
SNYTSPLGAA MLMNRLFTEG LIDDEKQSFI KNTLKECKTG VDRIAAPLLD KEGVVIAHKT
GSGYVNENGV LAAHNDVAYI CLPNNISYTL AVFVKDFKGN ESQASQYVAH ISAVVYSLLM
QTSVKS
//
