ID   SIPC_SALTI              Reviewed;         409 AA.
AC   Q56135; Q7AME1; Q7C7N2;
DT   25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 107.
DE   RecName: Full=Cell invasion protein SipC;
DE   AltName: Full=Effector protein SipC;
GN   Name=sipC; Synonyms=sspC; OrderedLocusNames=STY3007, t2786;
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   SUBCELLULAR LOCATION.
RC   STRAIN=GIFU 10007;
RX   PubMed=11293481; DOI=10.1111/j.1348-0421.2001.tb01283.x;
RA   Zhao L., Ezak T., Li Z.-Y., Kawamura Y., Hirose K., Watanabe H.;
RT   "Vi-Suppressed wild strain Salmonella typhi cultured in high osmolarity is
RT   hyperinvasive toward epithelial cells and destructive of Peyer's patches.";
RL   Microbiol. Immunol. 45:149-158(2001).
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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11293481}.
CC       Note=Secreted via the type III secretion system 1 (SPI-1 TTSS).
CC   -!- SIMILARITY: Belongs to the invasin protein C family. {ECO:0000305}.
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DR   EMBL; X82670; CAA57989.1; -; Genomic_DNA.
DR   EMBL; AE014613; AAO70347.1; -; Genomic_DNA.
DR   EMBL; AL513382; CAD05991.1; -; Genomic_DNA.
DR   PIR; S70215; S70215.
DR   RefSeq; NP_457278.1; NC_003198.1.
DR   RefSeq; WP_000909023.1; NZ_WSUR01000005.1.
DR   AlphaFoldDB; Q56135; -.
DR   STRING; 220341.16503962; -.
DR   EnsemblBacteria; AAO70347; AAO70347; t2786.
DR   KEGG; stt:t2786; -.
DR   KEGG; sty:STY3007; -.
DR   PATRIC; fig|220341.7.peg.3061; -.
DR   eggNOG; ENOG5032TZ4; Bacteria.
DR   HOGENOM; CLU_055996_0_0_6; -.
DR   OMA; MEIQNTK; -.
DR   Proteomes; UP000000541; Chromosome.
DR   Proteomes; UP000002670; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   InterPro; IPR005427; BacInvasinC.
DR   Pfam; PF09599; IpaC_SipC; 1.
DR   TIGRFAMs; TIGR02101; IpaC_SipC; 1.
PE   3: Inferred from homology;
KW   Actin-binding; Secreted; Virulence.
FT   CHAIN           1..409
FT                   /note="Cell invasion protein SipC"
FT                   /id="PRO_0000219859"
FT   REGION          1..119
FT                   /note="Actin-bundling"
FT                   /evidence="ECO:0000250"
FT   REGION          120..200
FT                   /note="Inserted into the host cell plasma membrane"
FT                   /evidence="ECO:0000250"
FT   REGION          201..409
FT                   /note="Actin-polymerization"
FT                   /evidence="ECO:0000250"
FT   REGION          350..378
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        350..368
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  43081 MW;  06FC92B345091E3B 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 SATESLGIKN SNKQISPEHQ AILSKRLESV
     ESDIRLEQNT MDMTRIDARK MQMTGDLIMK NSVTVGGIAG ASRQYAATQE RSEQQISQVN
     NRVASTASDE ARESSRKSTS LIQEMLKTME SINQSKASAL AAIAGNIRA