ID Q8KT51_9BACT Unreviewed; 321 AA.
AC Q8KT51;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 66.
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};
GN Name=cfxa2 {ECO:0000313|EMBL:AAM48125.1};
OS Hoylesella oralis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Hoylesella.
OX NCBI_TaxID=28134 {ECO:0000313|EMBL:AAM48125.1};
RN [1] {ECO:0000313|EMBL:AAM48125.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NI-113 {ECO:0000313|EMBL:AAM48125.1};
RX PubMed=12697645; DOI=10.1093/jac/dkg221;
RA Giraud-Morin C., Madinier I., Fosse T.;
RT "Sequence analysis of cfxA2-like beta-lactamases in Prevotella species.";
RL J. Antimicrob. Chemother. 51:1293-1296(2003).
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; AF504918; AAM48125.1; -; Genomic_DNA.
DR RefSeq; WP_063843241.1; NG_047638.1.
DR AlphaFoldDB; Q8KT51; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 9..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..289
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 321 AA; 35301 MW; 72EE7E72D9F5BCBF CRC64;
MEKNRKKQIV VLSIALVCIF ILVFSLFHKS ATKDSANPPL TNVLTDSISQ IVSACPGEIG
VAVIVNNRDT VKANNKSVYP MMSVFKVHQA LALCNDFDNK GISLDTLVNI NRDKLDPKTW
SPMLKDYSGP VISLTVRDLL RYTLTQSDNN ASNLMFKDMV NVAQTDSFIA TLIPRSSFQI
AYTEEEMSAD HNKAYSNYTS PLGAAMLMNR LVTEGLIDDE KQSFIKNTLK ECKTGVDRIA
APLLDKEGVV IAHKTGSGYV NENGVLAAHN DVAYICLPNN ISYTLAVFVK DFKGNESQAS
QYVAHISAVV YSLLMQTSVK S
//
