ID   SIPC_SALT1              Reviewed;         409 AA.
AC   D0ZV21;
DT   08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 50.
DE   RecName: Full=Cell invasion protein SipC;
DE   AltName: Full=Effector protein SipC;
GN   Name=sipC; OrderedLocusNames=STM14_3483;
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
RN   [2]
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).
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:10972831}.
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}.
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DR   EMBL; CP001363; ACY89897.1; -; Genomic_DNA.
DR   RefSeq; WP_000909019.1; NZ_CP043402.1.
DR   AlphaFoldDB; D0ZV21; -.
DR   EnsemblBacteria; ACY89897; ACY89897; STM14_3483.
DR   KEGG; seo:STM14_3483; -.
DR   PATRIC; fig|588858.6.peg.3204; -.
DR   HOGENOM; CLU_055996_0_0_6; -.
DR   OMA; MEIQNTK; -.
DR   BioCyc; SENT588858:STM14_RS15460-MON; -.
DR   PHI-base; PHI:3735; -.
DR   Proteomes; UP000002695; 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_0000406082"
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"
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