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   27-MAR-2024, entry version 154.
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};
GN   OrderedLocusNames=STM1444;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; 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; 99287-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 DNA-templated transcription; IBA:GO_Central.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_01819; HTH_type_SlyA; 1.
DR   InterPro; IPR000835; HTH_MarR-typ.
DR   InterPro; IPR039422; MarR/SlyA-like.
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   PANTHER; PTHR33164:SF64; TRANSCRIPTIONAL REGULATOR SLYA; 1.
DR   PANTHER; PTHR33164; TRANSCRIPTIONAL REGULATOR, MARR FAMILY; 1.
DR   Pfam; PF01047; MarR; 1.
DR   PRINTS; PR00598; HTHMARR.
DR   SMART; SM00347; HTH_MARR; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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
//