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 01-MAY-2013, entry version 111.
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 277:1453-1474(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).
CC -!- INDUCTION: Repressed by glucose.
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 -!- SIMILARITY: Contains 1 HTH luxR-type DNA-binding domain.
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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_000913.2.
DR RefSeq; YP_490173.1; NC_007779.1.
DR PDB; 2AVX; NMR; -; A=3-171.
DR PDBsum; 2AVX; -.
DR ProteinModelPortal; P07026; -.
DR SMR; P07026; 1-240.
DR IntAct; P07026; 4.
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 KO; K07782; -.
DR OMA; PAVAIFD; -.
DR ProtClustDB; PRK10188; -.
DR BioCyc; EcoCyc:PD02198; -.
DR BioCyc; ECOL316407:JW1901-MONOMER; -.
DR EvolutionaryTrace; P07026; -.
DR Genevestigator; P07026; -.
DR GO; GO:0005622; C:intracellular; IEA:InterPro.
DR GO; GO:0000156; F:phosphorelay response regulator activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
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:0035556; P:intracellular signal transduction; IEA:GOC.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:EcoCyc.
DR GO; GO:2000144; P:positive regulation of DNA-dependent transcription, initiation; IDA:EcoCyc.
DR GO; GO:0006351; P:transcription, DNA-dependent; 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; Bipartite_resp_reg_C-effector; 1.
DR SUPFAM; SSF75516; TF_LuxR_autoind-bd_dom; 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.
FT DNA_BIND 197 216 H-T-H motif (By similarity).
FT CONFLICT 120 128 TQYLMLPNR -> HSVFNAAQTG (in Ref. 1;
FT CAA27327).
FT CONFLICT 140 140 A -> R (in Ref. 1; CAA27327).
FT HELIX 5 19
FT HELIX 23 35
FT TURN 36 38
FT STRAND 42 48
FT STRAND 56 61
FT HELIX 65 73
FT HELIX 76 78
FT HELIX 81 83
FT TURN 85 87
FT STRAND 91 94
FT TURN 97 100
FT HELIX 104 113
FT STRAND 117 123
FT STRAND 130 138
FT HELIX 148 169
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
//
