SIPB_SALTI
ID SIPB_SALTI Reviewed; 593 AA.
AC Q56134; Q7AME0; Q7C7N1;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Cell invasion protein SipB;
DE AltName: Full=Effector protein SipB;
GN Name=sipB; OrderedLocusNames=STY3008, t2787;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=8801431; DOI=10.1111/j.1365-2958.1995.mmi_17040781.x;
RA Hermant D., Menard R., Arricau N., Parsot C., Popoff M.Y.;
RT "Functional conservation of the Salmonella and Shigella effectors of entry
RT into epithelial cells.";
RL Mol. Microbiol. 17:781-789(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [4]
RP FUNCTION IN CASPASE-1-DEPENDENT APOPTOSIS.
RC STRAIN=ATCC 700931 / Ty2;
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).
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 (By similarity). {ECO:0000250, ECO:0000269|PubMed:10051653}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- INTERACTION:
CC Q56134; P29452: Casp1; Xeno; NbExp=2; IntAct=EBI-489689, EBI-489700;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Host cell membrane
CC {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Secreted
CC via the type III secretion system 1 (SPI-1 TTSS) and inserted into the
CC host cell plasma membrane. {ECO:0000250}.
CC -!- DOMAIN: SipB membrane integration requires both hydrophobic domains and
CC the helical C-terminal region. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the invasin protein B family. {ECO:0000305}.
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DR EMBL; X82670; CAA57988.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD05992.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70348.1; -; Genomic_DNA.
DR PIR; S70216; S70216.
DR RefSeq; NP_457279.1; NC_003198.1.
DR RefSeq; WP_000245782.1; NZ_WSUR01000005.1.
DR AlphaFoldDB; Q56134; -.
DR SMR; Q56134; -.
DR IntAct; Q56134; 1.
DR STRING; 220341.16503963; -.
DR EnsemblBacteria; AAO70348; AAO70348; t2787.
DR KEGG; stt:t2787; -.
DR KEGG; sty:STY3008; -.
DR PATRIC; fig|220341.7.peg.3062; -.
DR eggNOG; ENOG502ZBCB; Bacteria.
DR HOGENOM; CLU_027418_0_0_6; -.
DR OMA; KFASHSI; -.
DR PHI-base; PHI:638; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 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 Coiled coil; Host cell membrane; Host membrane; Membrane; Secreted;
KW Transmembrane; Transmembrane helix; Virulence.
FT CHAIN 1..593
FT /note="Cell invasion protein SipB"
FT /id="PRO_0000219855"
FT TRANSMEM 320..354
FT /note="Helical"
FT /evidence="ECO:0000250"
FT TRANSMEM 408..427
FT /note="Helical"
FT /evidence="ECO:0000250"
FT COILED 151..208
FT /evidence="ECO:0000255"
FT COILED 287..314
FT /evidence="ECO:0000255"
SQ SEQUENCE 593 AA; 62421 MW; 8570D64343276639 CRC64;
MVNDASSISR SGYTQNPRLA EAAFEGVRKN TDFLKAADKA FKDVVATKAG DLKAGTKSGE
SAINTVGLKP PTDAAREKLS SEGQLTLLLG KLMTLLGDVS LSQLESRLAV WQAMIESQKE
MGIQVSKEFQ TALGEAQEAT DLYEASIKKT DTAKSVYDAA AKKLTQAQNK 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