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Database: UniProt
Entry: A6MFP3_STAAU
LinkDB: A6MFP3_STAAU
Original site: A6MFP3_STAAU 
ID   A6MFP3_STAAU            Unreviewed;       217 AA.
AC   A6MFP3;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 57.
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:ABK96861.1};
OS   Staphylococcus aureus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=1280 {ECO:0000313|EMBL:ABK96861.1};
RN   [1] {ECO:0000313|EMBL:ABK96861.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IS {ECO:0000313|EMBL:ABK96861.1};
RX   PubMed=17350771; DOI=10.1016/j.vetmic.2007.02.012;
RA   Malik S., Christensen H., Peng H., Barton M.D.;
RT   "Presence and diversity of the beta-lactamase gene in cat and dog
RT   staphylococci.";
RL   Vet. Microbiol. 123:162-168(2007).
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; DQ919093; ABK96861.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6MFP3; -.
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   PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR   PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 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}.
FT   DOMAIN          10..215
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABK96861.1"
FT   NON_TER         217
FT                   /evidence="ECO:0000313|EMBL:ABK96861.1"
SQ   SEQUENCE   217 AA;  24350 MW;  84DAD5D68D247D8A CRC64;
     LEKKYNAHIG VYALDTKSGK EVKFNSDKRF AYASTSKAIN SAILLEQVPY NKLNKKVHIN
     KDDIVAYSPI LEKYVGKDIT LKELIEASMT YSDNTANNKI IKEIGGIKKV KQRLKELGDK
     VTNPVRYEIE LNYYSPKSKK DTSTPAAFGK TLNKLIANGK LSKKNKNFLL DLMFNNKNGD
     TLIKDGVPKD YKVADKSGQA ITYASRNDVA FVYPKGQ
//
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