ID   SIPC_SALTS              Reviewed;         409 AA.
AC   E1WAC8; Q56020; Q56025; Q7CPX1;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Cell invasion protein SipC;
DE   AltName: Full=Effector protein SipC;
GN   Name=sipC; Synonyms=sspC; OrderedLocusNames=SL1344_2863;
OS   Salmonella typhimurium (strain SL1344).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=216597;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
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 [GENOMIC DNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL1344;
RX   PubMed=22538806; DOI=10.1073/pnas.1201061109;
RA   Kroger C., Dillon S.C., Cameron A.D., Papenfort K., Sivasankaran S.K.,
RA   Hokamp K., Chao Y., Sittka A., Hebrard M., Handler K., Colgan A.,
RA   Leekitcharoenphon P., Langridge G.C., Lohan A.J., Loftus B., Lucchini S.,
RA   Ussery D.W., Dorman C.J., Thomson N.R., Vogel J., Hinton J.C.;
RT   "The transcriptional landscape and small RNAs of Salmonella enterica
RT   serovar Typhimurium.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:E1277-E1286(2012).
CC   -!- FUNCTION: Actin-binding protein that interferes with host cell actin
CC       cytoskeleton. Nucleates actin polymerization and condensates actin
CC       filaments into cables (bundling). SipA potenciates SipC activity and
CC       both are required for an efficient bacterial internalization by the
CC       host cell (By similarity). {ECO:0000250}.
CC   -!- INTERACTION:
CC       E1WAC8; E1WAC8: sipC; NbExp=3; IntAct=EBI-6470515, EBI-6470515;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7608068}.
CC       Note=Secreted via the type III secretion system 1 (SPI-1 TTSS) and
CC       inserted into the host cell plasma membrane.
CC   -!- SIMILARITY: Belongs to the invasin protein C family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA75170.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U25631; AAA75170.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U30491; AAC43547.1; -; Genomic_DNA.
DR   EMBL; FQ312003; CBW18961.1; -; Genomic_DNA.
DR   PIR; S70548; S70548.
DR   RefSeq; WP_000909019.1; NZ_QASL01000017.1.
DR   AlphaFoldDB; E1WAC8; -.
DR   IntAct; E1WAC8; 5.
DR   EnsemblBacteria; CBW18961; CBW18961; SL1344_2863.
DR   KEGG; sey:SL1344_2863; -.
DR   PATRIC; fig|216597.6.peg.3185; -.
DR   HOGENOM; CLU_055996_0_0_6; -.
DR   OMA; MEIQNTK; -.
DR   Proteomes; UP000008962; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0045335; C:phagocytic vesicle; IMP:AgBase.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0019905; F:syntaxin binding; IPI:AgBase.
DR   GO; GO:0007015; P:actin filament organization; IMP:AgBase.
DR   GO; GO:0034067; P:protein localization to Golgi apparatus; IMP:AgBase.
DR   GO; GO:2000535; P:regulation of entry of bacterium into host cell; IMP:AgBase.
DR   GO; GO:0032880; P:regulation of protein localization; IMP:AgBase.
DR   InterPro; IPR005427; BacInvasinC.
DR   Pfam; PF09599; IpaC_SipC; 1.
DR   TIGRFAMs; TIGR02101; IpaC_SipC; 1.
PE   1: Evidence at protein level;
KW   Actin-binding; Secreted; Virulence.
FT   CHAIN           1..409
FT                   /note="Cell invasion protein SipC"
FT                   /id="PRO_0000406083"
FT   REGION          1..119
FT                   /note="Actin-bundling"
FT   REGION          120..200
FT                   /note="Inserted into the host cell plasma membrane"
FT   REGION          201..409
FT                   /note="Actin-polymerization"
FT   CONFLICT        73
FT                   /note="F -> S (in Ref. 1; AAA75170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        310
FT                   /note="T -> Y (in Ref. 1; AAA75170)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        313
FT                   /note="M -> I (in Ref. 1; AAA75170)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   409 AA;  42983 MW;  84FACCD1D5157245 CRC64;
     MLISNVGINP AAYLNNHSVE NSSQTASQSV SAKDILNSIG ISSSKVSDLG LSPTLSAPAP
     GVLTQTPGTI TSFLKASIQN TDMNQDLNAL ANNVTTKANE VVQTQLREQQ AEVGKFFDIS
     GMSSSAVALL AAANTLMLTL NQADSKLSGK LSLVSFDAAK TTASSMMREG MNALSGSISQ
     SALQLGITGV GAKLEYKGLQ NERGALKHNA AKIDKLTTES HSIKNVLNGQ NSVKLGAEGV
     DSLKSLNMKK TGTDATKNLN DATLKSNAGT SATESLGIKD SNKQISPEHQ AILSKRLESV
     ESDIRLEQNT MDMTRIDARK MQMTGDLIMK NSVTVGGIAG ASGQYAATQE RSEQQISQVN
     NRVASTASDE ARESSRKSTS LIQEMLKTME SINQSKASAL AAIAGNIRA