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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
 
 
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