SLYA_ECOLI
ID SLYA_ECOLI Reviewed; 144 AA.
AC P0A8W2; P55740;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Transcriptional regulator SlyA {ECO:0000255|HAMAP-Rule:MF_01819};
GN Name=slyA {ECO:0000255|HAMAP-Rule:MF_01819};
GN OrderedLocusNames=b1642, JW5267;
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=8544813; DOI=10.1007/bf00290573;
RA Ludwig A., Tengel C., Bauer S., Bubert A., Benz R., Mollenkopf H.-J.,
RA Goebel W.;
RT "SlyA, a regulatory protein from Salmonella typhimurium, induces a
RT haemolytic and pore-forming protein in Escherichia coli.";
RL Mol. Gen. Genet. 249:474-486(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=K12;
RX PubMed=8861216; DOI=10.1111/j.1365-2958.1996.tb02500.x;
RA Oscarsson J., Mizunoe Y., Uhlin B.E., Haydon D.;
RT "Induction of haemolytic activity in Escherichia coli by the slyA gene
RT product.";
RL Mol. Microbiol. 20:191-199(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=10027972; DOI=10.1046/j.1365-2958.1999.01196.x;
RA Ludwig A., Bauer S., Benz R., Bergmann B., Goebel W.;
RT "Analysis of the SlyA-controlled expression, subcellular localization and
RT pore-forming activity of a 34 kDa haemolysin (ClyA) from Escherichia coli
RT K-12.";
RL Mol. Microbiol. 31:557-567(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [5]
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 [6]
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 [7]
RP FUNCTION.
RX PubMed=11053378; DOI=10.1128/jb.182.22.6347-6357.2000;
RA Westermark M., Oscarsson J., Mizunoe Y., Urbonaviciene J., Uhlin B.E.;
RT "Silencing and activation of ClyA cytotoxin expression in Escherichia
RT coli.";
RL J. Bacteriol. 182:6347-6357(2000).
RN [8]
RP FUNCTION.
RX PubMed=12057949; DOI=10.1128/jb.184.13.3549-3559.2002;
RA Spory A., Bosserhoff A., von Rhein C., Goebel W., Ludwig A.;
RT "Differential regulation of multiple proteins of Escherichia coli and
RT Salmonella enterica serovar Typhimurium by the transcriptional regulator
RT SlyA.";
RL J. Bacteriol. 184:3549-3559(2002).
CC -!- FUNCTION: Transcription regulator that can specifically activate or
CC repress expression of target genes. Activates expression of genes such
CC as molecular chaperones (groL, groS, dnaK, grpE, and cbpA), proteins
CC involved in acid resistance (hdeA, hdeB, and gadA), the starvation
CC lipoprotein slp, virulence protein hlyE/clyA. Represses expression of
CC genes involved in the histidine biosynthetic pathway such as hisA,
CC hisB, hisD, hisF and hisG. Required for the activation of virulence
CC genes. {ECO:0000255|HAMAP-Rule:MF_01819, ECO:0000269|PubMed:11053378,
CC ECO:0000269|PubMed:12057949, ECO:0000269|PubMed:8861216}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01819}.
CC -!- SIMILARITY: Belongs to the SlyA family. {ECO:0000255|HAMAP-
CC Rule:MF_01819}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA09442.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAA72078.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ010965; CAA09442.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y11194; CAA72078.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC74714.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15403.2; -; Genomic_DNA.
DR PIR; S70929; S70929.
DR RefSeq; NP_416159.2; NC_000913.3.
DR RefSeq; WP_001296943.1; NZ_STEB01000003.1.
DR AlphaFoldDB; P0A8W2; -.
DR SMR; P0A8W2; -.
DR BioGRID; 4262957; 10.
DR STRING; 511145.b1642; -.
DR jPOST; P0A8W2; -.
DR PaxDb; P0A8W2; -.
DR PRIDE; P0A8W2; -.
DR EnsemblBacteria; AAC74714; AAC74714; b1642.
DR EnsemblBacteria; BAA15403; BAA15403; BAA15403.
DR GeneID; 66674466; -.
DR GeneID; 946167; -.
DR KEGG; ecj:JW5267; -.
DR KEGG; eco:b1642; -.
DR PATRIC; fig|1411691.4.peg.618; -.
DR EchoBASE; EB3184; -.
DR eggNOG; COG1846; Bacteria.
DR HOGENOM; CLU_083287_18_2_6; -.
DR InParanoid; P0A8W2; -.
DR OMA; CSNDRRA; -.
DR PhylomeDB; P0A8W2; -.
DR BioCyc; EcoCyc:G6882-MON; -.
DR PRO; PR:P0A8W2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IMP:EcoliWiki.
DR GO; GO:2000143; P:negative regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:2000144; P:positive regulation of DNA-templated transcription, initiation; IDA:EcoCyc.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:CACAO.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR Gene3D; 1.10.10.10; -; 1.
DR HAMAP; MF_01819; HTH_type_SlyA; 1.
DR InterPro; IPR000835; HTH_MarR-typ.
DR InterPro; IPR023187; Tscrpt_reg_MarR-type_CS.
DR InterPro; IPR023071; Tscrpt_reg_SlyA.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF01047; MarR; 1.
DR PRINTS; PR00598; HTHMARR.
DR SMART; SM00347; HTH_MARR; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS01117; HTH_MARR_1; 1.
DR PROSITE; PS50995; HTH_MARR_2; 1.
PE 3: Inferred from homology;
KW Activator; DNA-binding; Reference proteome; Repressor; Transcription;
KW Transcription regulation; Virulence.
FT CHAIN 1..144
FT /note="Transcriptional regulator SlyA"
FT /id="PRO_0000054383"
FT DOMAIN 2..135
FT /note="HTH marR-type"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01819"
FT DNA_BIND 49..72
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01819"
FT CONFLICT 121
FT /note="E -> Q (in Ref. 2; CAA72078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 16353 MW; A07293A45BEF6CAB CRC64;
MESPLGSDLA RLVRIWRALI DHRLKPLELT QTHWVTLHNI HQLPPDQSQI QLAKAIGIEQ
PSLVRTLDQL EEKGLISRQT CASDRRAKRI KLTEKAEPLI SEMEAVINKT RAEILHGISA
EELEQLITLI AKLEHNIIEL QAKG
