BLAI_STAAU
ID BLAI_STAAU Reviewed; 126 AA.
AC P0A042; P18415;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Penicillinase repressor;
DE AltName: Full=Beta-lactamase repressor protein;
DE AltName: Full=Regulatory protein BlaI;
GN Name=blaI; Synonyms=penI;
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=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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1861992; DOI=10.1093/nar/19.14.4000;
RA Wang P.Z., Projan S.J., Novick R.P.;
RT "Nucleotide sequence of beta-lactamase regulatory genes from staphylococcal
RT plasmid pI258.";
RL Nucleic Acids Res. 19:4000-4000(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RN4;
RX PubMed=1444307; DOI=10.1128/aac.36.10.2265;
RA Smith M.C., Murray B.E.;
RT "Sequence analysis of the beta-lactamase repressor from Staphylococcus
RT aureus and hybridization studies with two beta-lactamase-producing isolates
RT of Enterococcus faecalis.";
RL Antimicrob. Agents Chemother. 36:2265-2269(1992).
RN [4]
RP PROTEIN SEQUENCE OF 102-110, INACTIVATION BY PROTEOLYTIC CLEAVAGE, AND
RP MUTAGENESIS OF 101-ASN-PHE-102.
RX PubMed=11239156; DOI=10.1126/science.1055144;
RA Zhang H.Z., Hackbarth C.J., Chansky K.M., Chambers H.F.;
RT "A proteolytic transmembrane signaling pathway and resistance to beta-
RT lactams in staphylococci.";
RL Science 291:1962-1965(2001).
RN [5]
RP INACTIVATION BY PROTEOLYTIC CLEAVAGE.
RX PubMed=10499277; DOI=10.1111/j.1574-6968.1999.tb08687.x;
RA Lewis R.A., Curnock S.P., Dyke K.G.H.;
RT "Proteolytic cleavage of the repressor (BlaI) of beta-lactamase synthesis
RT in Staphylococcus aureus.";
RL FEMS Microbiol. Lett. 178:271-275(1999).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH DNA, AND SUBUNIT.
RX PubMed=15716455; DOI=10.1128/jb.187.5.1833-1844.2005;
RA Safo M.K., Zhao Q., Ko T.-P., Musayev F.N., Robinson H., Scarsdale N.,
RA Wang A.H.-J., Archer G.L.;
RT "Crystal structures of the BlaI repressor from Staphylococcus aureus and
RT its complex with DNA: insights into transcriptional regulation of the bla
RT and mec operons.";
RL J. Bacteriol. 187:1833-1844(2005).
CC -!- FUNCTION: Transcriptional repressor that constitutively blocks
CC expression of beta-lactamase. Binds DNA as a dimer (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15716455}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Upon exposure to beta-lactams, the protease BlaR1 is activated and
CC cleaves BlaI at a single site. This proteolytic cleavage impairs
CC dimerization and abolishes repressor activity.
CC -!- SIMILARITY: Belongs to the BlaI transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; X52734; CAA36951.1; -; Genomic_DNA.
DR EMBL; M62650; AAA26603.1; -; Genomic_DNA.
DR EMBL; M92376; AAA26605.1; -; Genomic_DNA.
DR PIR; S11782; S11782.
DR RefSeq; NP_878025.1; NC_005054.1.
DR RefSeq; WP_001284656.1; NZ_WWCF01000102.1.
DR RefSeq; YP_003329486.1; NC_013550.1.
DR RefSeq; YP_006937604.1; NC_013319.1.
DR RefSeq; YP_006937749.1; NC_013323.1.
DR RefSeq; YP_006938265.1; NC_013337.1.
DR RefSeq; YP_006938772.1; NC_013352.1.
DR RefSeq; YP_008709797.1; NC_022598.1.
DR PDB; 1SD4; X-ray; 2.00 A; A/B=3-126.
DR PDB; 1XSD; X-ray; 2.70 A; A=3-126.
DR PDBsum; 1SD4; -.
DR PDBsum; 1XSD; -.
DR AlphaFoldDB; P0A042; -.
DR SMR; P0A042; -.
DR GeneID; 58063711; -.
DR OMA; FFMKKND; -.
DR EvolutionaryTrace; P0A042; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0010468; P:regulation of gene expression; IDA:CACAO.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005650; BlaI_family.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34134; PTHR34134; 1.
DR Pfam; PF03965; Penicillinase_R; 1.
DR PIRSF; PIRSF019455; CopR_AtkY; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Plasmid; Repressor; Transcription; Transcription regulation;
KW Transposable element.
FT CHAIN 1..126
FT /note="Penicillinase repressor"
FT /id="PRO_0000062793"
FT DNA_BIND 7..71
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 74..126
FT /note="Important for dimerization"
FT /evidence="ECO:0000250"
FT SITE 101..102
FT /note="Cleavage"
FT MUTAGEN 101..102
FT /note="NF->AA: Abolishes proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:11239156"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:1SD4"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:1SD4"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:1SD4"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1SD4"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1SD4"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:1SD4"
FT HELIX 75..91
FT /evidence="ECO:0007829|PDB:1SD4"
FT HELIX 95..104
FT /evidence="ECO:0007829|PDB:1SD4"
FT HELIX 110..123
FT /evidence="ECO:0007829|PDB:1SD4"
SQ SEQUENCE 126 AA; 14876 MW; E0759E83A5183117 CRC64;
MANKQVEISM AEWDVMNIIW GKKSVSANEI VVEIQKYKEV SDKTIRTLIT RLYKKEIIKR
YKSENIYFYS SNIKEDDIKM KTAKTFLNKL YGGDMKSLVL NFAKNEELNN KEIEELRDIL
NDISKK