SIPB_SALTY
ID SIPB_SALTY Reviewed; 593 AA.
AC Q56019; Q56024; Q7CPX0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Cell invasion protein SipB;
DE AltName: Full=Effector protein SipB;
GN Name=sipB; Synonyms=sspB; OrderedLocusNames=STM2885;
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=SL1344;
RX PubMed=7608068; DOI=10.1128/jb.177.14.3965-3971.1995;
RA Kaniga K., Tucker S.C., Trollinger D., Galan J.E.;
RT "Homologs of the Shigella IpaB and IpaC invasins are required for
RT Salmonella typhimurium entry into cultured epithelial cells.";
RL J. Bacteriol. 177:3965-3971(1995).
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 305-593.
RC STRAIN=SL1344;
RX PubMed=8748032; DOI=10.1111/j.1365-2958.1995.mmi_18030479.x;
RA Hueck C.J., Hantman M.J., Bajaj V., Johnston C., Lee C.A., Miller S.I.;
RT "Salmonella typhimurium secreted invasion determinants are homologous to
RT Shigella Ipa proteins.";
RL Mol. Microbiol. 18:479-490(1995).
RN [4]
RP FUNCTION IN CASPASE-1-DEPENDENT APOPTOSIS.
RC STRAIN=C5, and SL1344;
RX PubMed=10051653; DOI=10.1073/pnas.96.5.2396;
RA Hersh D., Monack D.M., Smith M.R., Ghori N., Falkow S., Zychlinsky A.;
RT "The Salmonella invasin SipB induces macrophage apoptosis by binding to
RT caspase-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:2396-2401(1999).
RN [5]
RP SUBUNIT, AND MEMBRANE-FUSION ACTIVITY.
RC STRAIN=SJW1103;
RX PubMed=10972796; DOI=10.1046/j.1365-2958.2000.02027.x;
RA Hayward R.D., McGhie E.J., Koronakis V.;
RT "Membrane fusion activity of purified SipB, a Salmonella surface protein
RT essential for mammalian cell invasion.";
RL Mol. Microbiol. 37:727-739(2000).
RN [6]
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=10972831; DOI=10.1046/j.1365-2958.2000.02066.x;
RA Scherer C.A., Cooper E., Miller S.I.;
RT "The Salmonella type III secretion translocon protein SspC is inserted into
RT the epithelial cell plasma membrane upon infection.";
RL Mol. Microbiol. 37:1133-1145(2000).
RN [7]
RP REGULATION BY INVE.
RX PubMed=12169593; DOI=10.1128/jb.184.17.4699-4708.2002;
RA Kubori T., Galan J.E.;
RT "Salmonella type III secretion-associated protein InvE controls
RT translocation of effector proteins into host cells.";
RL J. Bacteriol. 184:4699-4708(2002).
RN [8]
RP TOPOLOGY.
RC STRAIN=SJW1103;
RX PubMed=12068811; DOI=10.1046/j.1365-2958.2002.02958.x;
RA McGhie E.J., Hume P.J., Hayward R.D., Torres J., Koronakis V.;
RT "Topology of the Salmonella invasion protein SipB in a model bilayer.";
RL Mol. Microbiol. 44:1309-1321(2002).
RN [9]
RP FUNCTION IN CASPASE-1-INDEPENDENT APOPTOSIS.
RC STRAIN=SL1344;
RX PubMed=14662750; DOI=10.1083/jcb.200309161;
RA Hernandez L.D., Pypaert M., Flavell R.A., Galan J.E.;
RT "A Salmonella protein causes macrophage cell death by inducing autophagy.";
RL J. Cell Biol. 163:1123-1131(2003).
CC -!- FUNCTION: Required for entry into the host cell through presentation or
CC delivery of SipC at the host cell plasma membrane. Along with SipC, is
CC necessary for the transfer of other effector proteins into the host
CC cell. Induces macrophage apoptosis either by binding and activating the
CC proapoptotic enzyme caspase-1 (caspase-1 dependent), resulting in the
CC release of interleukin-1 beta active form, or by disrupting
CC mitochondria and inducing autophagy (caspase-1 independent). The former
CC is dependent of its membrane-fusion activity. The SipBC complex, in
CC association with its chaperone SicA, is regulated by binding of InvE.
CC {ECO:0000269|PubMed:10051653, ECO:0000269|PubMed:14662750}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10972796}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10972831}. Host cell
CC membrane {ECO:0000269|PubMed:10972831}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:10972831}. Note=Secreted via the type III secretion
CC system 1 (SPI-1 TTSS), inserted into the phagosomal membrane and
CC subsequently released into the host cell cytoplasm.
CC -!- DOMAIN: SipB membrane integration requires both hydrophobic domains and
CC the helical C-terminal region.
CC -!- SIMILARITY: Belongs to the invasin protein B family. {ECO:0000305}.
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DR EMBL; U25631; AAA75169.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21765.1; -; Genomic_DNA.
DR EMBL; U30491; AAC43546.1; -; Genomic_DNA.
DR PIR; S70547; S70547.
DR RefSeq; NP_461806.1; NC_003197.2.
DR RefSeq; WP_000245788.1; NC_003197.2.
DR PDB; 3TUL; X-ray; 2.79 A; A/B/C/D=81-237.
DR PDBsum; 3TUL; -.
DR AlphaFoldDB; Q56019; -.
DR SMR; Q56019; -.
DR STRING; 99287.STM2885; -.
DR TCDB; 1.C.36.3.2; the bacterial type iii-target cell pore (iiitcp) family.
DR PaxDb; Q56019; -.
DR EnsemblBacteria; AAL21765; AAL21765; STM2885.
DR GeneID; 1254408; -.
DR KEGG; stm:STM2885; -.
DR PATRIC; fig|99287.12.peg.3041; -.
DR HOGENOM; CLU_027418_0_0_6; -.
DR OMA; KFASHSI; -.
DR BioCyc; SENT99287:STM2885-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:AgBase.
DR InterPro; IPR032391; SipB_N.
DR InterPro; IPR006972; SseC.
DR InterPro; IPR003895; T3SS_invasion_prot_B.
DR Pfam; PF04888; SseC; 1.
DR Pfam; PF16535; T3SSipB; 1.
DR PRINTS; PR01375; BACINVASINB.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Host cell membrane; Host membrane; Membrane;
KW Reference proteome; Secreted; Transmembrane; Transmembrane helix;
KW Virulence.
FT CHAIN 1..593
FT /note="Cell invasion protein SipB"
FT /id="PRO_0000219856"
FT TRANSMEM 320..354
FT /note="Helical"
FT TRANSMEM 408..427
FT /note="Helical"
FT COILED 151..208
FT /evidence="ECO:0000255"
FT COILED 287..314
FT /evidence="ECO:0000255"
FT HELIX 85..99
FT /evidence="ECO:0007829|PDB:3TUL"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3TUL"
FT TURN 119..122
FT /evidence="ECO:0007829|PDB:3TUL"
FT HELIX 129..171
FT /evidence="ECO:0007829|PDB:3TUL"
FT HELIX 183..221
FT /evidence="ECO:0007829|PDB:3TUL"
SQ SEQUENCE 593 AA; 62451 MW; 63A5D5949D85BA46 CRC64;
MVNDASSISR SGYTQNPRLA EAAFEGVRKN TDFLKAADKA FKDVVATKAG DLKAGTKSGE
SAINTVGLKP PTDAAREKLS SEGQLTLLLG KLMTLLGDVS LSQLESRLAV WQAMIESQKE
MGIQVSKEFQ TALGEAQEAT DLYEASIKKT DTAKSVYDAA TKKLTQAQNK LQSLDPADPG
YAQAEAAVEQ AGKEATEAKE ALDKATDATV KAGTDAKAKA EKADNILTKF QGTANAASQN
QVSQGEQDNL SNVARLTMLM AMFIEIVGKN TEESLQNDLA LFNALQEGRQ AEMEKKSAEF
QEETRKAEET NRIMGCIGKV LGALLTIVSV VAAVFTGGAS LALAAVGLAV MVADEIVKAA
TGVSFIQQAL NPIMEHVLKP LMELIGKAIT KALEGLGVDK KTAEMAGSIV GAIVAAIAMV
AVIVVVAVVG KGAAAKLGNA LSKMMGETIK KLVPNVLKQL AQNGSKLFTQ GMQRITSGLG
NVGSKMGLQT NALSKELVGN TLNKVALGME VTNTAAQSAG GVAEGVFIKN ASEALADFML
ARFAMDQIQQ WLKQSVEIFG ENQKVTAELQ KAMSSAVQQN ADASRFILRQ SRA
