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SSEI_SALTY
ID   SSEI_SALTY              Reviewed;         322 AA.
AC   Q8ZQ79; Q9KIC1; Q9KIK1;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Secreted effector protein SseI;
GN   Name=sseI; Synonyms=srfH; OrderedLocusNames=STM1051;
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=10844662; DOI=10.1046/j.1365-2958.2000.01902.x;
RA   Worley M.J., Ching K.H., Heffron F.;
RT   "Salmonella SsrB activates a global regulon of horizontally acquired
RT   genes.";
RL   Mol. Microbiol. 36:749-761(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND SECRETION VIA
RP   TYPE III SECRETION SYSTEM.
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=10861017; DOI=10.1073/pnas.97.13.7539;
RA   Miao E.A., Miller S.I.;
RT   "A conserved amino acid sequence directing intracellular type III secretion
RT   by Salmonella typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:7539-7544(2000).
RN   [3]
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   [4]
RP   FUNCTION, AND INTERACTION WITH HOST TRIP6.
RC   STRAIN=ATCC 14028s / SGSG 2262;
RX   PubMed=17095609; DOI=10.1073/pnas.0604054103;
RA   Worley M.J., Nieman G.S., Geddes K., Heffron F.;
RT   "Salmonella typhimurium disseminates within its host by manipulating the
RT   motility of infected cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:17915-17920(2006).
RN   [5]
RP   FUNCTION, INTERACTION WITH HOST IQGAP1, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF CYS-178; HIS-216 AND ASP-231.
RC   STRAIN=SL1344;
RX   PubMed=19956712; DOI=10.1371/journal.ppat.1000671;
RA   McLaughlin L.M., Govoni G.R., Gerke C., Gopinath S., Peng K., Laidlaw G.,
RA   Chien Y.H., Jeong H.W., Li Z., Brown M.D., Sacks D.B., Monack D.;
RT   "The Salmonella SPI2 effector SseI mediates long-term systemic infection by
RT   modulating host cell migration.";
RL   PLoS Pathog. 5:E1000671-E1000671(2009).
CC   -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC       promote bacterial survival in host tissues. This protein is required to
CC       maintain a long-term chronic systemic infection in mice. It inhibits
CC       normal cell migration of primary macrophages and dendritic cells, by a
CC       mechanism that involves interaction with the host factor IQGAP1, an
CC       important regulator of the cytoskeleton and cell migration. Also
CC       accelerates the systemic spread of infection from the gastrointestinal
CC       tract to the bloodstream, probably by interacting with host TRIP6.
CC       {ECO:0000269|PubMed:17095609, ECO:0000269|PubMed:19956712}.
CC   -!- SUBUNIT: Interacts with host IQGAP1 and host TRIP6 (thyroid receptor-
CC       interacting protein 6). {ECO:0000269|PubMed:17095609,
CC       ECO:0000269|PubMed:19956712}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10861017}. Host
CC       cytoplasm {ECO:0000269|PubMed:10861017, ECO:0000269|PubMed:19956712}.
CC       Note=Secreted via type III secretion system 2 (SPI-2 TTSS), and
CC       delivered into the host cytoplasm. Colocalizes with IQGAP1 and actin at
CC       the cell periphery. {ECO:0000269|PubMed:10861017}.
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DR   EMBL; AF231470; AAF73990.2; -; Genomic_DNA.
DR   EMBL; AF236075; AAF82082.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL19985.1; -; Genomic_DNA.
DR   RefSeq; WP_001533476.1; NC_003197.2.
DR   PDB; 4G29; X-ray; 1.70 A; A=137-322.
DR   PDB; 4G2B; X-ray; 2.05 A; A/B=137-322.
DR   PDBsum; 4G29; -.
DR   PDBsum; 4G2B; -.
DR   AlphaFoldDB; Q8ZQ79; -.
DR   SMR; Q8ZQ79; -.
DR   DIP; DIP-61315N; -.
DR   IntAct; Q8ZQ79; 1.
DR   STRING; 90371.CY43_05385; -.
DR   PaxDb; Q8ZQ79; -.
DR   EnsemblBacteria; AAL19985; AAL19985; STM1051.
DR   PATRIC; fig|99287.12.peg.1115; -.
DR   HOGENOM; CLU_077951_0_0_6; -.
DR   OMA; SADEWAC; -.
DR   BioCyc; SENT99287:STM1051-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   InterPro; IPR028907; Tox-PLDMTX_dom.
DR   Pfam; PF15645; Tox-PLDMTX; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host cytoplasm; Reference proteome; Secreted; Virulence.
FT   CHAIN           1..322
FT                   /note="Secreted effector protein SseI"
FT                   /id="PRO_0000391491"
FT   MUTAGEN         178
FT                   /note="C->A: Loss of activity. No change in IQGAP1
FT                   binding."
FT                   /evidence="ECO:0000269|PubMed:19956712"
FT   MUTAGEN         216
FT                   /note="H->A: Does not affect regulation of macrophage
FT                   migration."
FT                   /evidence="ECO:0000269|PubMed:19956712"
FT   MUTAGEN         231
FT                   /note="D->A: Does not affect regulation of macrophage
FT                   migration."
FT                   /evidence="ECO:0000269|PubMed:19956712"
FT   CONFLICT        103
FT                   /note="D -> G (in Ref. 1; AAF73990 and 2; AAF82082)"
FT                   /evidence="ECO:0000305"
FT   TURN            150..153
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           154..162
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           165..172
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           178..191
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   STRAND          195..207
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   STRAND          214..223
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   STRAND          226..231
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           234..237
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   TURN            238..241
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   STRAND          249..252
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           253..262
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   STRAND          268..276
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           277..283
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           291..293
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   STRAND          300..302
FT                   /evidence="ECO:0007829|PDB:4G29"
FT   HELIX           306..312
FT                   /evidence="ECO:0007829|PDB:4G29"
SQ   SEQUENCE   322 AA;  36831 MW;  1A896A8995660094 CRC64;
     MPFHIGSGCL PAIISNRRIY RIAWSDTPPE MSSWEKMKEF FCSTHQAEAL ECIWTICHPP
     AGTTREDVVS RFELLRTLAY DGWEENIHSG LHGENYFCIL DEDSQEILSV TLDDVGNYTV
     NCQGYSETHH LTMATEPGVE RTDITYNLTS DIDAAAYLEE LKQNPIINNK IMNPVGQCES
     LMTPVSNFMN EKGFDNIRYR GIFIWDKPTE EIPTNHFAVV GNKEGKDYVF DVSAHQFENR
     GMSNLNGPLI LSADEWVCKY RMATRRKLIY YTDFSNSSIA ANAYDALPRE LESESMAGKV
     FVTSPRWFNT FKKQKYSLIG KM
 
 
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