ID D2J8J7_STAEP Unreviewed; 281 AA.
AC D2J8J7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
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=blaZ {ECO:0000313|EMBL:ADA61768.1};
GN ORFNames=SAP045A_036 {ECO:0000313|EMBL:ADA61768.1};
OS Staphylococcus epidermidis.
OG Plasmid SAP045A {ECO:0000313|EMBL:ADA61768.1}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282 {ECO:0000313|EMBL:ADA61768.1};
RN [1] {ECO:0000313|EMBL:ADA61768.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CDC9 {ECO:0000313|EMBL:ADA61768.1};
RC PLASMID=SAP045A {ECO:0000313|EMBL:ADA61768.1};
RA Gill J., Borman J., Shetty J., Hostetler J., Durkin S., Montgomery B.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADA61768.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CDC9 {ECO:0000313|EMBL:ADA61768.1};
RC PLASMID=SAP045A {ECO:0000313|EMBL:ADA61768.1};
RA Summers A.O., Shearer J., Wireman J.;
RL Submitted (DEC-2009) 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; GQ900402; ADA61768.1; -; Genomic_DNA.
DR RefSeq; WP_000733270.1; NZ_WBRL01000010.1.
DR RefSeq; YP_006938977.1; NC_013374.1.
DR AlphaFoldDB; D2J8J7; -.
DR GeneID; 58050741; -.
DR PATRIC; fig|1282.1338.peg.953; -.
DR OrthoDB; 9784149at2; -.
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 Plasmid {ECO:0000313|EMBL:ADA61768.1};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 39..256
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 281 AA; 31262 MW; A69F68C8934025DC CRC64;
MKKLIFLIAI ALVLSACNSN SPHAKELNDL EKKYNAHIGV YALDTKSGKE VKFNSDKRFA
YASTSKAINS AILLEQVPYN KLNKKIHINK DDIVAYSPIL EKYVGKDITL KELIEASMTY
SDNTANNKII KEIGGNKKVK QRLKGLGDKV TNPVRYEIEL NYYSPKSKKD TSTPAAFGKT
LNKLIANGKL SKENKKFLLD LMLNNKSGDT LIKDGVSKDC KVADKSGQAI TYASRNDVAF
VYPKGQSEPI VLVIFTNKDN KSDKPNDKLI SETAKSVMKE F
//
