BLAC_STAAU
ID BLAC_STAAU Reviewed; 281 AA.
AC P00807;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Beta-lactamase;
DE EC=3.5.2.6;
DE AltName: Full=Penicillinase;
DE Flags: Precursor;
GN Name=blaZ;
OS Staphylococcus aureus.
OG Plasmid pI258.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PC-1; PLASMID=pI258;
RX PubMed=3488540; DOI=10.1093/nar/14.14.5940;
RA Chan P.T.;
RT "Nucleotide sequence of the Staphylococcus aureus PC1 beta-lactamase
RT gene.";
RL Nucleic Acids Res. 14:5940-5940(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SK456; TRANSPOSON=Tn4002;
RX PubMed=2555777; DOI=10.1093/nar/17.21.8854;
RA Gillspie M.T., Skurray R.A.;
RT "Nucleotide sequence of the blaZ gene of the Staphylococcus aureus beta-
RT lactamase transposon Tn4002.";
RL Nucleic Acids Res. 17:8854-8854(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NCTC 9789 / PS80; TRANSPOSON=Tn552;
RX PubMed=2170815; DOI=10.1111/j.1365-2958.1990.tb00669.x;
RA Rowland S.J., Dyke K.G.H.;
RT "Tn552, a novel transposable element from Staphylococcus aureus.";
RL Mol. Microbiol. 4:961-975(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC PLASMID=pI258;
RX PubMed=3104315; DOI=10.1128/jb.169.4.1763-1766.1987;
RA Wang P.-Z., Novick R.P.;
RT "Nucleotide sequence and expression of the beta-lactamase gene from
RT Staphylococcus aureus plasmid pI258 in Escherichia coli, Bacillus subtilis,
RT and Staphylococcus aureus.";
RL J. Bacteriol. 169:1763-1766(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-47.
RX PubMed=6793593; DOI=10.1016/s0021-9258(19)68589-3;
RA McLaughlin J.R., Murray C.L., Rabinowitz J.C.;
RT "Unique features in the ribosome binding site sequence of the Gram-positive
RT Staphylococcus aureus beta-lactamase gene.";
RL J. Biol. Chem. 256:11283-11291(1981).
RN [6]
RP PROTEIN SEQUENCE OF 25-281.
RX PubMed=1218078; DOI=10.1042/bj1510197;
RA Ambler R.P.;
RT "The amino acid sequence of Staphylococcus aureus penicillinase.";
RL Biochem. J. 151:197-218(1975).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=3107125; DOI=10.1126/science.3107125;
RA Herzberg O., Moult J.;
RT "Bacterial resistance to beta-lactam antibiotics: crystal structure of
RT beta-lactamase from Staphylococcus aureus PC1 at 2.5-A resolution.";
RL Science 236:694-701(1987).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=2005620; DOI=10.1016/0022-2836(91)90527-d;
RA Herzberg O.;
RT "Refined crystal structure of beta-lactamase from Staphylococcus aureus PC1
RT at 2.0-A resolution.";
RL J. Mol. Biol. 217:701-719(1991).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9521648; DOI=10.1021/bi972127f;
RA Banerjee S., Pieper U., Kapadia G., Pannell L.K., Herzberg O.;
RT "Role of the omega-loop in the activity, substrate specificity, and
RT structure of class A beta-lactamase.";
RL Biochemistry 37:3286-3296(1998).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=10436083; DOI=10.1093/protein/12.7.573;
RA Chen C.C., Herzberg O.;
RT "Relocation of the catalytic carboxylate group in class A beta-lactamase:
RT the structure and function of the mutant enzyme
RT Glu166-->Gln:Asn170-->Asp.";
RL Protein Eng. 12:573-579(1999).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU10101};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; X04121; CAA27733.1; -; Genomic_DNA.
DR EMBL; X16471; CAA34491.1; -; Genomic_DNA.
DR EMBL; M15526; AAA98239.1; -; Genomic_DNA.
DR EMBL; X52734; CAA36953.1; -; Genomic_DNA.
DR PIR; A01002; PNSAP.
DR RefSeq; NP_878023.1; NC_005054.1.
DR RefSeq; WP_000733283.1; NZ_WWCF01000102.1.
DR RefSeq; YP_003329488.1; NC_013550.1.
DR RefSeq; YP_006937602.1; NC_013319.1.
DR RefSeq; YP_006937751.1; NC_013323.1.
DR RefSeq; YP_006938263.1; NC_013337.1.
DR RefSeq; YP_006938770.1; NC_013352.1.
DR RefSeq; YP_008709799.1; NC_022598.1.
DR PDB; 1ALQ; X-ray; 1.80 A; A=24-244.
DR PDB; 1BLC; X-ray; 2.20 A; A=25-281.
DR PDB; 1BLH; X-ray; 2.30 A; A=25-281.
DR PDB; 1BLP; X-ray; 2.30 A; A=25-281.
DR PDB; 1DJA; X-ray; 1.90 A; A=25-281.
DR PDB; 1DJB; X-ray; 2.10 A; A=25-281.
DR PDB; 1DJC; X-ray; 2.00 A; A=25-281.
DR PDB; 1GHI; X-ray; 2.30 A; A=25-281.
DR PDB; 1GHM; X-ray; 1.86 A; A=25-281.
DR PDB; 1GHP; X-ray; 1.76 A; A=25-281.
DR PDB; 1KGE; X-ray; 2.00 A; A=25-281.
DR PDB; 1KGF; X-ray; 2.20 A; A=25-281.
DR PDB; 1KGG; X-ray; 2.30 A; A=24-281.
DR PDB; 1OME; X-ray; 2.30 A; A/B=25-281.
DR PDB; 1PIO; X-ray; 2.80 A; A/B=25-281.
DR PDB; 3BLM; X-ray; 2.00 A; A=25-281.
DR PDB; 6WGR; X-ray; 1.88 A; A/B/C=25-281.
DR PDBsum; 1ALQ; -.
DR PDBsum; 1BLC; -.
DR PDBsum; 1BLH; -.
DR PDBsum; 1BLP; -.
DR PDBsum; 1DJA; -.
DR PDBsum; 1DJB; -.
DR PDBsum; 1DJC; -.
DR PDBsum; 1GHI; -.
DR PDBsum; 1GHM; -.
DR PDBsum; 1GHP; -.
DR PDBsum; 1KGE; -.
DR PDBsum; 1KGF; -.
DR PDBsum; 1KGG; -.
DR PDBsum; 1OME; -.
DR PDBsum; 1PIO; -.
DR PDBsum; 3BLM; -.
DR PDBsum; 6WGR; -.
DR AlphaFoldDB; P00807; -.
DR SMR; P00807; -.
DR BindingDB; P00807; -.
DR ChEMBL; CHEMBL4114; -.
DR DrugBank; DB02642; [[N-(Benzyloxycarbonyl)Amino]Methyl]Phosphate.
DR DrugBank; DB11367; Cefroxadine.
DR DrugBank; DB04133; Degraded Cephaloridine.
DR DrugBank; DB09324; Sulbactam.
DR DrugCentral; P00807; -.
DR GeneID; 58063709; -.
DR OMA; EWMKGNA; -.
DR SABIO-RK; P00807; -.
DR EvolutionaryTrace; P00807; -.
DR PRO; PR:P00807; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 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; PTHR35333; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR Pfam; PF08139; LPAM_1; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing; Hydrolase;
KW Plasmid; Signal; Transposable element.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303,
FT ECO:0000269|PubMed:1218078"
FT CHAIN 25..281
FT /note="Beta-lactamase"
FT /id="PRO_0000017020"
FT ACT_SITE 63
FT /note="Acyl-ester intermediate"
FT BINDING 225..227
FT /ligand="substrate"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1ALQ"
FT HELIX 26..33
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 37..44
FT /evidence="ECO:0007829|PDB:1GHP"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 50..54
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 65..76
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 79..83
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 85..88
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 90..92
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 136..145
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 159..161
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:1OME"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1GHP"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 212..215
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 230..232
FT /evidence="ECO:0007829|PDB:1OME"
FT STRAND 235..242
FT /evidence="ECO:0007829|PDB:1GHP"
FT STRAND 250..257
FT /evidence="ECO:0007829|PDB:1GHP"
FT HELIX 267..278
FT /evidence="ECO:0007829|PDB:1GHP"
SQ SEQUENCE 281 AA; 31349 MW; F82A836773C275FE CRC64;
MKKLIFLIVI ALVLSACNSN SSHAKELNDL EKKYNAHIGV YALDTKSGKE VKFNSDKRFA
YASTSKAINS AILLEQVPYN KLNKKVHINK DDIVAYSPIL EKYVGKDITL KALIEASMTY
SDNTANNKII KEIGGIKKVK QRLKELGDKV TNPVRYEIEL NYYSPKSKKD TSTPAAFGKT
LNKLIANGKL SKENKKFLLD LMLNNKSGDT LIKDGVPKDY KVADKSGQAI TYASRNDVAF
VYPKGQSEPI VLVIFTNKDN KSDKPNDKLI SETAKSVMKE F
