ID   SIPB_SALDU              Reviewed;         593 AA.
AC   Q79BT1;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 52.
DE   RecName: Full=Cell invasion protein SipB;
DE   AltName: Full=Effector protein SipB;
GN   Name=sipB;
OS   Salmonella dublin.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=98360;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2229;
RA   Mullan P.B., Gautier A.V., Wood M.W., Edwards M.H., Jones B.V.,
RA   Galyov E.E.;
RT   "Sip invasins of Salmonella dublin are involved in macrophage cytotoxicity
RT   and mouse virulence.";
RL   Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250}.
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; U66877; AAB06795.1; -; Genomic_DNA.
DR   RefSeq; WP_000245788.1; NZ_VDCP01000001.1.
DR   AlphaFoldDB; Q79BT1; -.
DR   SMR; Q79BT1; -.
DR   PRIDE; Q79BT1; -.
DR   PATRIC; fig|98360.39.peg.2686; -.
DR   OMA; KFASHSI; -.
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   3: Inferred from homology;
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_0000219854"
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;  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