SSEA_SALTY
ID SSEA_SALTY Reviewed; 108 AA.
AC O84944; Q7CQM2;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Type III secretion system chaperone SseA;
DE Short=TTSS chaperone SseA;
DE AltName: Full=Secretion system effector A;
GN Name=sseA; OrderedLocusNames=STM1397;
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], INDUCTION, 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, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=SL1344;
RX PubMed=12787732; DOI=10.1016/s1286-4579(03)00094-7;
RA Coombes B.K., Brown N.F., Kujat-Choy S., Vallance B.A., Finlay B.B.;
RT "SseA is required for translocation of Salmonella pathogenicity island-2
RT effectors into host cells.";
RL Microbes Infect. 5:561-570(2003).
RN [5]
RP FUNCTION AS A CHAPERONE, AND BINDING TO SSEB AND SSED.
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 FUNCTION AS A CHAPERONE, SUBCELLULAR LOCATION, AND BINDING TO SSEB.
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 BINDING TO SSEB AND SSED, AND DOMAIN.
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).
CC -!- FUNCTION: Functions as a type III secretion system (TTSS) chaperone,
CC which is required for SseB and SseD accumulation and secretion. May
CC have a direct role in secretion of SseB and SseD, or may facilitate
CC their correct folding, for efficient secretion and function. Required
CC for survival and replication within epithelial cells and macrophages.
CC {ECO:0000269|PubMed:12603739, ECO:0000269|PubMed:12724372,
CC ECO:0000269|PubMed:12787732}.
CC -!- SUBUNIT: Binds to SseB and SseD.
CC -!- INTERACTION:
CC O84944; Q7BVH7: sseB; NbExp=4; IntAct=EBI-2030631, EBI-2030613;
CC O84944; Q9R803: sseD; NbExp=2; IntAct=EBI-2030631, EBI-2272067;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:12603739,
CC ECO:0000305|PubMed:12787732}. Note=May associate with the inner
CC membrane.
CC -!- INDUCTION: Expression is regulated by the two-component regulatory
CC system SsrA/SsrB. {ECO:0000269|PubMed:9786193}.
CC -!- DOMAIN: The N-terminal region is dispensable for binding and
CC stabilizing SseB, but is essential for export of SseB to the surface of
CC the bacterium. {ECO:0000269|PubMed:15256549}.
CC -!- DISRUPTION PHENOTYPE: Mutant is severely attenuated in virulence.
CC {ECO:0000269|PubMed:12787732, ECO:0000269|PubMed:9786193}.
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DR EMBL; AJ224892; CAA12184.1; -; Genomic_DNA.
DR EMBL; AF020808; AAC28878.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20321.1; -; Genomic_DNA.
DR RefSeq; NP_460362.1; NC_003197.2.
DR RefSeq; WP_001738219.1; NC_003197.2.
DR AlphaFoldDB; O84944; -.
DR SMR; O84944; -.
DR IntAct; O84944; 3.
DR STRING; 99287.STM1397; -.
DR PaxDb; O84944; -.
DR PRIDE; O84944; -.
DR EnsemblBacteria; AAL20321; AAL20321; STM1397.
DR GeneID; 1252915; -.
DR KEGG; stm:STM1397; -.
DR PATRIC; fig|99287.12.peg.1481; -.
DR HOGENOM; CLU_2208196_0_0_6; -.
DR OMA; KNREPDT; -.
DR BioCyc; SENT99287:STM1397-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Chaperone; Coiled coil; Cytoplasm; Reference proteome; Virulence.
FT CHAIN 1..108
FT /note="Type III secretion system chaperone SseA"
FT /id="PRO_0000391714"
FT COILED 69..97
FT /evidence="ECO:0000255"
SQ SEQUENCE 108 AA; 12449 MW; 5C58323413648E9E CRC64;
MMIKKKAAFS EYRDLEQSYM QLNHCLKKFH QIRAKVSQQL AERAESPKNS RETESILHNL
FPQGVAGVNQ EAEKDLKKIV SLFKQLEVRL KQLNAQAPVE IPSGKTKR
