SDIA_ECOLI
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 25-MAY-2022, entry version 156.
DE RecName: Full=Regulatory protein SdiA;
GN Name=sdiA; OrderedLocusNames=b1916, JW1901;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
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 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., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT 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., Mau B.,
RA 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 MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION.
RX PubMed=1915297; DOI=10.1002/j.1460-2075.1991.tb04900.x;
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 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 between
RT 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., Wright P.E.,
RA Dyson H.J.;
RT "Structure of the Escherichia coli quorum sensing protein SdiA: activation
RT 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 autoinducer
CC oxoC6). {ECO:0000269|PubMed:18560382, 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 endogenously it
CC should be able to bind to a number of different AI-1 autoinducers,
CC which would enable it to detect other bacteria. This was shown to be
CC 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}.
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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; WP_001152715.1; NZ_LN832404.1.
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 AlphaFoldDB; P07026; -.
DR BMRB; P07026; -.
DR SMR; P07026; -.
DR BioGRID; 4259602; 108.
DR BioGRID; 850778; 3.
DR IntAct; P07026; 8.
DR STRING; 511145.b1916; -.
DR ChEMBL; CHEMBL4523168; -.
DR DrugBank; DB07928; N-(2-OXOTETRAHYDROFURAN-3-YL)OCTANAMIDE.
DR PaxDb; P07026; -.
DR PRIDE; P07026; -.
DR EnsemblBacteria; AAC74983; AAC74983; b1916.
DR EnsemblBacteria; BAA15736; BAA15736; BAA15736.
DR GeneID; 946421; -.
DR KEGG; ecj:JW1901; -.
DR KEGG; eco:b1916; -.
DR PATRIC; fig|1411691.4.peg.333; -.
DR EchoBASE; EB0928; -.
DR eggNOG; COG2197; Bacteria.
DR HOGENOM; CLU_072786_7_1_6; -.
DR InParanoid; P07026; -.
DR OMA; NHTVDWY; -.
DR PhylomeDB; P07026; -.
DR BioCyc; EcoCyc:PD02198; -.
DR EvolutionaryTrace; P07026; -.
DR PRO; PR:P07026; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR CDD; cd06170; LuxR_C_like; 1.
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; IPR036693; TF_LuxR_autoind-bd_dom_sf.
DR InterPro; IPR000792; Tscrpt_reg_LuxR_C.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
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; DNA-binding;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..240
FT /note="Regulatory protein SdiA"
FT /id="PRO_0000184187"
FT DOMAIN 173..238
FT /note="HTH luxR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT DNA_BIND 197..216
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00411"
FT CONFLICT 120..128
FT /note="TQYLMLPNR -> HSVFNAAQTG (in Ref. 1; CAA27327)"
FT /evidence="ECO:0000305"
FT CONFLICT 140
FT /note="A -> R (in Ref. 1; CAA27327)"
FT /evidence="ECO:0000305"
FT HELIX 6..19
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 23..36
FT /evidence="ECO:0007829|PDB:4LFU"
FT STRAND 40..47
FT /evidence="ECO:0007829|PDB:4LFU"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:4LFU"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 65..73
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4LFU"
FT STRAND 92..94
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 104..112
FT /evidence="ECO:0007829|PDB:4LFU"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:4LFU"
FT STRAND 130..138
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 147..167
FT /evidence="ECO:0007829|PDB:4LFU"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 197..204
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 208..222
FT /evidence="ECO:0007829|PDB:4LFU"
FT HELIX 227..236
FT /evidence="ECO:0007829|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
