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Database: UniProt
Entry: P07026
LinkDB: P07026
Original site: P07026 
ID   SDIA_ECOLI              Reviewed;         240 AA.
AC   P07026; P76313;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   26-NOV-2014, entry version 123.
DE   RecName: Full=Regulatory protein SdiA;
GN   Name=sdiA; OrderedLocusNames=b1916, JW1901;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3515318; DOI=10.1093/nar/14.5.2301;
RA   Sharma S., Stark T.F., Beattie W.G., Moses R.E.;
RT   "Multiple control elements for the uvrC gene unit of Escherichia
RT   coli.";
RL   Nucleic Acids Res. 14:2301-2318(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C.,
RA   Yamamoto Y., Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION.
RX   PubMed=1915297;
RA   Wang X., de Boer P.A.J., Rothfield L.I.;
RT   "A factor that positively regulates cell division by activating
RT   transcription of the major cluster of essential cell division genes of
RT   Escherichia coli.";
RL   EMBO J. 10:3363-3372(1991).
RN   [6]
RP   ROLE IN YDIV REGULATION, REPRESSION BY GLUCOSE, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=K12 / W3110 / ZK126;
RX   PubMed=18560382; DOI=10.1038/cr.2008.67;
RA   Zhou X., Meng X., Sun B.;
RT   "An EAL domain protein and cyclic AMP contribute to the interaction
RT   between the two quorum sensing systems in Escherichia coli.";
RL   Cell Res. 18:937-948(2008).
RN   [7]
RP   STRUCTURE BY NMR OF 3-171 IN COMPLEX WITH AUTOINDUCER, AND BINDING OF
RP   HOMOSERINE LACTONE DERIVATIVES.
RX   PubMed=16307757; DOI=10.1016/j.jmb.2005.10.041;
RA   Yao Y., Martinez-Yamout M.A., Dickerson T.J., Brogan A.P.,
RA   Wright P.E., Dyson H.J.;
RT   "Structure of the Escherichia coli quorum sensing protein SdiA:
RT   activation of the folding switch by acyl homoserine lactones.";
RL   J. Mol. Biol. 355:262-273(2006).
CC   -!- FUNCTION: Activates cell division by specifically increasing
CC       transcription from one of the two promoters that lie immediately
CC       upstream of the ftsQAZ gene cluster. Activates ydiV expression in
CC       response to extracellular autoinducer AI-1 (Vibrio fischeri
CC       autoinducer oxoC6). {ECO:0000269|PubMed:18560382,
CC       ECO:0000269|PubMed:1915297}.
CC   -!- INDUCTION: Repressed by glucose. {ECO:0000269|PubMed:18560382}.
CC   -!- DOMAIN: Binding to the autoinducer occurs via the N-terminal 170
CC       residues; as E.coli does not produce LuxI autoinducers
CC       endogenously it should be able to bind to a number of different
CC       AI-1 autoinducers, which would enable it to detect other bacteria.
CC       This was shown to be the case.
CC   -!- DISRUPTION PHENOTYPE: A double sdiA/ydiV deletion mutant leads to
CC       decreased cAMP levels which inhibits quorum sensing system 2.
CC       {ECO:0000269|PubMed:18560382}.
CC   -!- SIMILARITY: Contains 1 HTH luxR-type DNA-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00411}.
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DR   EMBL; X03691; CAA27327.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74983.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15736.1; -; Genomic_DNA.
DR   PIR; A64955; QQECU1.
DR   RefSeq; NP_416426.1; NC_000913.3.
DR   RefSeq; YP_490173.1; NC_007779.1.
DR   PDB; 2AVX; NMR; -; A=1-171.
DR   PDB; 4LFU; X-ray; 2.26 A; A=1-240.
DR   PDB; 4LGW; X-ray; 2.70 A; A=1-240.
DR   PDBsum; 2AVX; -.
DR   PDBsum; 4LFU; -.
DR   PDBsum; 4LGW; -.
DR   ProteinModelPortal; P07026; -.
DR   SMR; P07026; 5-240.
DR   IntAct; P07026; 8.
DR   STRING; 511145.b1916; -.
DR   PaxDb; P07026; -.
DR   PRIDE; P07026; -.
DR   EnsemblBacteria; AAC74983; AAC74983; b1916.
DR   EnsemblBacteria; BAA15736; BAA15736; BAA15736.
DR   GeneID; 12930608; -.
DR   GeneID; 946421; -.
DR   KEGG; ecj:Y75_p1887; -.
DR   KEGG; eco:b1916; -.
DR   PATRIC; 32119167; VBIEscCol129921_1998.
DR   EchoBASE; EB0928; -.
DR   EcoGene; EG10935; sdiA.
DR   eggNOG; COG2771; -.
DR   HOGENOM; HOG000111053; -.
DR   InParanoid; P07026; -.
DR   KO; K07782; -.
DR   OMA; VMPPEMK; -.
DR   OrthoDB; EOG6P8TQG; -.
DR   PhylomeDB; P07026; -.
DR   BioCyc; EcoCyc:PD02198; -.
DR   BioCyc; ECOL316407:JW1901-MONOMER; -.
DR   EvolutionaryTrace; P07026; -.
DR   PRO; PR:P07026; -.
DR   Genevestigator; P07026; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0032467; P:positive regulation of cytokinesis; IMP:EcoCyc.
DR   GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.10; -; 1.
DR   Gene3D; 3.30.450.80; -; 1.
DR   InterPro; IPR016032; Sig_transdc_resp-reg_C-effctor.
DR   InterPro; IPR005143; TF_LuxR_autoind-bd_dom.
DR   InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR   InterPro; IPR011991; WHTH_DNA-bd_dom.
DR   Pfam; PF03472; Autoind_bind; 1.
DR   Pfam; PF00196; GerE; 1.
DR   PRINTS; PR00038; HTHLUXR.
DR   SMART; SM00421; HTH_LUXR; 1.
DR   SUPFAM; SSF46894; SSF46894; 1.
DR   SUPFAM; SSF75516; SSF75516; 1.
DR   PROSITE; PS00622; HTH_LUXR_1; 1.
DR   PROSITE; PS50043; HTH_LUXR_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Activator; Cell cycle; Cell division; Complete proteome;
KW   DNA-binding; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    240       Regulatory protein SdiA.
FT                                /FTId=PRO_0000184187.
FT   DOMAIN      173    238       HTH luxR-type. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   DNA_BIND    197    216       H-T-H motif. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00411}.
FT   CONFLICT    120    128       TQYLMLPNR -> HSVFNAAQTG (in Ref. 1;
FT                                CAA27327). {ECO:0000305}.
FT   CONFLICT    140    140       A -> R (in Ref. 1; CAA27327).
FT                                {ECO:0000305}.
FT   HELIX         6     19       {ECO:0000244|PDB:4LFU}.
FT   HELIX        23     36       {ECO:0000244|PDB:4LFU}.
FT   STRAND       40     47       {ECO:0000244|PDB:4LFU}.
FT   STRAND       51     54       {ECO:0000244|PDB:4LFU}.
FT   STRAND       57     61       {ECO:0000244|PDB:4LFU}.
FT   HELIX        65     73       {ECO:0000244|PDB:4LFU}.
FT   HELIX        76     78       {ECO:0000244|PDB:4LFU}.
FT   HELIX        81     83       {ECO:0000244|PDB:4LFU}.
FT   HELIX        85     87       {ECO:0000244|PDB:4LFU}.
FT   STRAND       92     94       {ECO:0000244|PDB:4LFU}.
FT   HELIX        97    100       {ECO:0000244|PDB:4LFU}.
FT   HELIX       104    112       {ECO:0000244|PDB:4LFU}.
FT   STRAND      117    124       {ECO:0000244|PDB:4LFU}.
FT   STRAND      130    138       {ECO:0000244|PDB:4LFU}.
FT   HELIX       147    167       {ECO:0000244|PDB:4LFU}.
FT   TURN        171    173       {ECO:0000244|PDB:4LFU}.
FT   HELIX       182    192       {ECO:0000244|PDB:4LFU}.
FT   HELIX       197    204       {ECO:0000244|PDB:4LFU}.
FT   HELIX       208    222       {ECO:0000244|PDB:4LFU}.
FT   HELIX       227    236       {ECO:0000244|PDB:4LFU}.
SQ   SEQUENCE   240 AA;  28117 MW;  C04CCC50C06135C4 CRC64;
     MQDKDFFSWR RTMLLRFQRM ETAEEVYHEI ELQAQQLEYD YYSLCVRHPV PFTRPKVAFY
     TNYPEAWVSY YQAKNFLAID PVLNPENFSQ GHLMWNDDLF SEAQPLWEAA RAHGLRRGVT
     QYLMLPNRAL GFLSFSRCSA REIPILSDEL QLKMQLLVRE SLMALMRLND EIVMTPEMNF
     SKREKEILRW TAEGKTSAEI AMILSISENT VNFHQKNMQK KINAPNKTQV ACYAAATGLI
//
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