ID   SSEB_SALTY              Reviewed;         196 AA.
AC   Q7BVH7; Q7CQM1;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Secreted effector protein SseB;
DE   AltName: Full=Secretion system effector B;
GN   Name=sseB; OrderedLocusNames=STM1398;
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], AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=9786193; DOI=10.1046/j.1365-2958.1998.01047.x;
RA   Hensel M., Shea J.E., Waterman S.R., Mundy R., Nikolaus T., Banks G.,
RA   Vazquez-Torres A., Gleeson C., Fang F.C., Holden D.W.;
RT   "Genes encoding putative effector proteins of the type III secretion system
RT   of Salmonella pathogenicity island 2 are required for bacterial virulence
RT   and proliferation in macrophages.";
RL   Mol. Microbiol. 30:163-174(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SL1344;
RX   PubMed=9786194; DOI=10.1046/j.1365-2958.1998.01048.x;
RA   Cirillo D.M., Valdivia R.H., Monack D.M., Falkow S.;
RT   "Macrophage-dependent induction of the Salmonella pathogenicity island 2
RT   type III secretion system and its role in intracellular survival.";
RL   Mol. Microbiol. 30:175-188(1998).
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, SUBUNIT, SUBCELLULAR LOCATION, AND SECRETION VIA TYPE III
RP   SECRETION SYSTEM.
RC   STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=11567004; DOI=10.1128/jb.183.20.6036-6045.2001;
RA   Nikolaus T., Deiwick J., Rappl C., Freeman J.A., Schroder W., Miller S.I.,
RA   Hensel M.;
RT   "SseBCD proteins are secreted by the type III secretion system of
RT   Salmonella pathogenicity island 2 and function as a translocon.";
RL   J. Bacteriol. 183:6036-6045(2001).
RN   [5]
RP   INTERACTION WITH SSEA.
RC   STRAIN=ATCC 14028 / SGSC 2980 / CDC 6516-60 / NCTC 12023;
RX   PubMed=12724372; DOI=10.1099/mic.0.26190-0;
RA   Ruiz-Albert J., Mundy R., Yu X.J., Beuzon C.R., Holden D.W.;
RT   "SseA is a chaperone for the SseB and SseD translocon components of the
RT   Salmonella pathogenicity-island-2-encoded type III secretion system.";
RL   Microbiology 149:1103-1111(2003).
RN   [6]
RP   INTERACTION WITH SSEA.
RC   STRAIN=SL1344;
RX   PubMed=12603739; DOI=10.1046/j.1365-2958.2003.03373.x;
RA   Zurawski D.V., Stein M.A.;
RT   "SseA acts as the chaperone for the SseB component of the Salmonella
RT   pathogenicity island 2 translocon.";
RL   Mol. Microbiol. 47:1341-1351(2003).
RN   [7]
RP   INTERACTION WITH SSEA.
RC   STRAIN=SL1344;
RX   PubMed=15256549; DOI=10.1099/mic.0.26997-0;
RA   Zurawski D.V., Stein M.A.;
RT   "The SPI2-encoded SseA chaperone has discrete domains required for SseB
RT   stabilization and export, and binds within the C-terminus of SseB and
RT   SseD.";
RL   Microbiology 150:2055-2068(2004).
RN   [8]
RP   ROLE IN SPVB EXPORT, AND DISRUPTION PHENOTYPE.
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=18248436; DOI=10.1111/j.1574-695x.2007.00364.x;
RA   Browne S.H., Hasegawa P., Okamoto S., Fierer J., Guiney D.G.;
RT   "Identification of Salmonella SPI-2 secretion system components required
RT   for SpvB-mediated cytotoxicity in macrophages and virulence in mice.";
RL   FEMS Immunol. Med. Microbiol. 52:194-201(2008).
CC   -!- FUNCTION: Effector proteins function to alter host cell physiology and
CC       promote bacterial survival in host tissues. May act as a translocator
CC       that mediates translocation of SPI-2 TTSS effector proteins from
CC       intraphagosomal bacterial cells into the host cells. SseB is required
CC       for correct localization of SseC and SseD on the bacterial cell
CC       surface. {ECO:0000269|PubMed:11567004, ECO:0000269|PubMed:18248436}.
CC   -!- SUBUNIT: May form a complex with SseC and SseD. Binds to the chaperone
CC       SseA. {ECO:0000269|PubMed:11567004}.
CC   -!- INTERACTION:
CC       Q7BVH7; O84944: sseA; NbExp=4; IntAct=EBI-2030613, EBI-2030631;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11567004}. Cell
CC       surface {ECO:0000269|PubMed:11567004}. Note=Secreted via type III
CC       secretion system 2 (SPI-2 TTSS). After secretion, localizes mainly on
CC       the surface of the bacterial cell.
CC   -!- DISRUPTION PHENOTYPE: Mutant is severely attenuated in virulence.
CC       Disruption prevents SpvB-induced F-actin depolymerization in human
CC       macrophages without affecting intra-bacterial SpvB protein levels.
CC       {ECO:0000269|PubMed:18248436, ECO:0000269|PubMed:9786193}.
CC   -!- SIMILARITY: Belongs to the EspA/SseB family. {ECO:0000305}.
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DR   EMBL; AJ224892; CAA12185.1; -; Genomic_DNA.
DR   EMBL; AF020808; AAC28879.1; -; Genomic_DNA.
DR   EMBL; AE006468; AAL20322.1; -; Genomic_DNA.
DR   RefSeq; NP_460363.1; NC_003197.2.
DR   RefSeq; WP_000094422.1; NC_003197.2.
DR   AlphaFoldDB; Q7BVH7; -.
DR   IntAct; Q7BVH7; 2.
DR   STRING; 99287.STM1398; -.
DR   TCDB; 1.C.36.5.1; the bacterial type iii-target cell pore (iiitcp) family.
DR   PaxDb; Q7BVH7; -.
DR   EnsemblBacteria; AAL20322; AAL20322; STM1398.
DR   GeneID; 1252916; -.
DR   KEGG; stm:STM1398; -.
DR   PATRIC; fig|99287.12.peg.1482; -.
DR   HOGENOM; CLU_091357_0_0_6; -.
DR   OMA; WGEISTM; -.
DR   BioCyc; SENT99287:STM1398-MON; -.
DR   PHI-base; PHI:2622; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:AgBase.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IDA:UniProtKB.
DR   InterPro; IPR005095; EspA.
DR   InterPro; IPR035074; EspA/CesA-like.
DR   Pfam; PF03433; EspA; 1.
DR   SUPFAM; SSF116927; SSF116927; 1.
PE   1: Evidence at protein level;
KW   Protein transport; Reference proteome; Secreted; Transport; Virulence.
FT   CHAIN           1..196
FT                   /note="Secreted effector protein SseB"
FT                   /id="PRO_0000391715"
SQ   SEQUENCE   196 AA;  21495 MW;  CD38B8995323DF67 CRC64;
     MSSGNILWGS QNPIVFKNSF GVSNADTGSQ DDLSQQNPFA EGYGVLLILL MVIQAIANNK
     FIEVQKNAER ARNTQEKSNE MDEVIAKAAK GDAKTKEEVP EDVIKYMRDN GILIDGMTID
     DYMAKYGDHG KLDKGGLQAI KAALDNDANR NTDLMSQGQI TIQKMSQELN AVLTQLTGLI
     SKWGEISSMI AQKTYS