SLYA_SALTY
ID SLYA_SALTY Reviewed; 144 AA.
AC P40676;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 3.
DT 25-MAY-2022, entry version 146.
DE RecName: Full=Transcriptional regulator SlyA {ECO:0000255|HAMAP-Rule:MF_01819};
DE AltName: Full=Cytolysin SlyA;
DE AltName: Full=Salmolysin;
GN Name=slyA {ECO:0000255|HAMAP-Rule:MF_01819}; OrderedLocusNames=STM1444;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=8290552; DOI=10.1073/pnas.91.2.489;
RA Libby S.J., Goebel W., Ludwig A., Buchmeier N., Bowe F., Fang F.C.,
RA Guiney D.G., Songer J.G., Heffron F.;
RT "A cytolysin encoded by Salmonella is required for survival within
RT macrophages.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:489-493(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION.
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 [4]
RP SIMILARITY TO MARR FAMILY.
RX PubMed=7783629; DOI=10.1111/j.1365-2958.1995.tb02272.x;
RA Dehoux P., Cossart P.;
RT "Homologies between salmolysin and some bacterial regulatory proteins.";
RL Mol. Microbiol. 15:591-591(1995).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=9284144; DOI=10.1128/iai.65.9.3725-3730.1997;
RA Buchmeier N., Bossie S., Chen C.-Y., Fang F.C., Guiney D.G., Libby S.J.;
RT "SlyA, a transcriptional regulator of Salmonella typhimurium, is required
RT for resistance to oxidative stress and is expressed in the intracellular
RT environment of macrophages.";
RL Infect. Immun. 65:3725-3730(1997).
RN [6]
RP HOMODIMERIZATION.
RX PubMed=11882648; DOI=10.1074/jbc.m110178200;
RA Stapleton M.R., Norte V.A., Read R.C., Green J.;
RT "Interaction of the Salmonella typhimurium transcription and virulence
RT factor SlyA with target DNA and identification of members of the SlyA
RT regulon.";
RL J. Biol. Chem. 277:17630-17637(2002).
RN [7]
RP INDUCTION.
RX PubMed=12775687; DOI=10.1128/jb.185.12.3508-3514.2003;
RA Norte V.A., Stapleton M.R., Green J.;
RT "PhoP-responsive expression of the Salmonella enterica serovar typhimurium
RT slyA gene.";
RL J. Bacteriol. 185:3508-3514(2003).
CC -!- FUNCTION: Transcription regulator that can specifically activate or
CC repress expression of target genes. Required for virulence and survival
CC in the macrophage environment. Probably activates expression of ispA,
CC xseB genes, and of omp operon. {ECO:0000255|HAMAP-Rule:MF_01819,
CC ECO:0000269|PubMed:8544813, ECO:0000269|PubMed:9284144}.
CC -!- SUBUNIT: Homodimer.
CC -!- INDUCTION: During infection of the host cells. Down-regulated by
CC itself. Activated by Mg(2+) starvation in a phoP dependent manner.
CC {ECO:0000269|PubMed:12775687, ECO:0000269|PubMed:9284144}.
CC -!- SIMILARITY: Belongs to the SlyA family. {ECO:0000255|HAMAP-
CC Rule:MF_01819}.
CC -!- CAUTION: Was originally thought to be a toxin with hemolytic and
CC cytolytic activity. {ECO:0000305|PubMed:8290552}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58796.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAL20366.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U03842; AAA58796.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE006468; AAL20366.1; ALT_INIT; Genomic_DNA.
DR PIR; A36874; A36874.
DR RefSeq; NP_460407.3; NC_003197.2.
DR PDB; 3DEU; X-ray; 2.30 A; A/B=2-144.
DR PDB; 3Q5F; X-ray; 2.96 A; A/B=1-144.
DR PDB; 3QPT; X-ray; 2.40 A; A=1-144.
DR PDBsum; 3DEU; -.
DR PDBsum; 3Q5F; -.
DR PDBsum; 3QPT; -.
DR AlphaFoldDB; P40676; -.
DR SMR; P40676; -.
DR DIP; DIP-48666N; -.
DR STRING; 99287.STM1444; -.
DR PaxDb; P40676; -.
DR EnsemblBacteria; AAL20366; AAL20366; STM1444.
DR GeneID; 1252962; -.
DR KEGG; stm:STM1444; -.
DR PATRIC; fig|99287.12.peg.1527; -.
DR HOGENOM; CLU_083287_18_2_6; -.
DR PhylomeDB; P40676; -.
DR EvolutionaryTrace; P40676; -.
DR PHI-base; PHI:2678; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Activator; DNA-binding; Reference proteome; Repressor;
KW Transcription; Transcription regulation; Virulence.
FT CHAIN 1..144
FT /note="Transcriptional regulator SlyA"
FT /id="PRO_0000054393"
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 97..98
FT /note="DA -> EP (in Ref. 1; AAA58796)"
FT /evidence="ECO:0000305"
FT HELIX 5..23
FT /evidence="ECO:0007829|PDB:3DEU"
FT TURN 24..28
FT /evidence="ECO:0007829|PDB:3DEU"
FT HELIX 31..42
FT /evidence="ECO:0007829|PDB:3DEU"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:3DEU"
FT HELIX 49..56
FT /evidence="ECO:0007829|PDB:3DEU"
FT HELIX 60..72
FT /evidence="ECO:0007829|PDB:3DEU"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:3DEU"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:3Q5F"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:3DEU"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:3DEU"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:3DEU"
FT HELIX 120..139
FT /evidence="ECO:0007829|PDB:3DEU"
SQ SEQUENCE 144 AA; 16422 MW; 2D37EB004F2D7439 CRC64;
MESPLGSDLA RLVRIWRALI DHRLKPLELT QTHWVTLHNI HQLPPDQSQI QLAKAIGIEQ
PSLVRTLDQL EDKGLISRQT CASDRRAKRI KLTEKADALI AEMEEVIHKT RGEILAGISS
EEIELLIKLI AKLEHNIMEL HSHD
