ID Q6UIV2_STAAU Unreviewed; 179 AA.
AC Q6UIV2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=blaZ {ECO:0000313|EMBL:AAR12671.1};
OS Staphylococcus aureus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280 {ECO:0000313|EMBL:AAR12671.1};
RN [1] {ECO:0000313|EMBL:AAR12671.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sweden41 {ECO:0000313|EMBL:AAR12671.1};
RA Vintov J., Aarestrup F.M., Olsen J.E.;
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAR12671.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Sweden41 {ECO:0000313|EMBL:AAR12671.1};
RX PubMed=16449305; DOI=10.1093/jac/dki492;
RA Olsen J.E., Christensen H., Aarestrup F.M.;
RT "Diversity and evolution of blaZ from Staphylococcus aureus and coagulase-
RT negative staphylococci.";
RL J. Antimicrob. Chemother. 57:450-460(2006).
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; AY369347; AAR12671.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6UIV2; -.
DR MEROPS; S11.A01; -.
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 InterPro; IPR012640; Membr_lipoprot_lipid_attach_CS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR Pfam; PF08139; LPAM_1; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..179
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004280591"
FT DOMAIN 39..177
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 179
FT /evidence="ECO:0000313|EMBL:AAR12671.1"
SQ SEQUENCE 179 AA; 20098 MW; CB928ED88CD238B6 CRC64;
MKKLIFLIAI ALVLSACNSN SPHAKKLNDL EKKYNAHIGV YALDTKSGKE VKFNSDKRFA
YASTSKAINS AILLEQIPYN KLNKKIHINK DDIVAYSPIL EKYVGKDITL KELIEASMTY
SDNTANNKII KEIGGIKKVK QRLKELGDKV TNPVRYEIEL NYYSPKSKKD TSTPAAFGK
//