ID   SCTC2_SALT1             Reviewed;         497 AA.
AC   D0ZWR9;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=SPI-2 type 3 secretion system secretin {ECO:0000305};
DE            Short=T3SS-2 secretin {ECO:0000305};
DE   AltName: Full=Outer membrane protein SpiA;
DE   AltName: Full=Type III secretion system outer membrane protein SpiA;
DE   Flags: Precursor;
GN   Name=sctC2 {ECO:0000255|HAMAP-Rule:MF_02219}; Synonyms=spiA, ssaC;
GN   OrderedLocusNames=STM14_1689;
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   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=10406797; DOI=10.1093/emboj/18.14.3924;
RA   Uchiya K., Barbieri M.A., Funato K., Shah A.H., Stahl P.D., Groisman E.A.;
RT   "A Salmonella virulence protein that inhibits cellular trafficking.";
RL   EMBO J. 18:3924-3933(1999).
CC   -!- FUNCTION: Component of the type III secretion system (T3SS), also
CC       called injectisome, which is used to inject bacterial effector proteins
CC       into eukaryotic host cells (PubMed:10406797). Forms a ring-shaped
CC       multimeric structure with an apparent central pore in the outer
CC       membrane (By similarity). Required for secretion of some type III-
CC       secreted effectors including the SpvB exotoxin (PubMed:10406797).
CC       {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000269|PubMed:10406797}.
CC   -!- SUBUNIT: The core secretion machinery of the T3SS is composed of
CC       approximately 20 different proteins, including cytoplasmic components,
CC       a base, an export apparatus and a needle. This subunit is part of the
CC       base, which anchors the injectisome in the bacterial cell envelope.
CC       Forms a stable homooligomeric complex. {ECO:0000255|HAMAP-
CC       Rule:MF_02219}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|HAMAP-
CC       Rule:MF_02219, ECO:0000269|PubMed:10406797}.
CC   -!- DISRUPTION PHENOTYPE: Does not survive in murine macrophages, although
CC       it can invade epithelial cells. The SpiC protein is not exported into
CC       host macrophage cells. {ECO:0000269|PubMed:10406797}.
CC   -!- SIMILARITY: Belongs to the bacterial secretin family. T3SS SctC
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02219, ECO:0000305}.
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DR   EMBL; CP001363; ACY88167.1; -; Genomic_DNA.
DR   RefSeq; WP_000261284.1; NZ_CP043402.1.
DR   AlphaFoldDB; D0ZWR9; -.
DR   SMR; D0ZWR9; -.
DR   EnsemblBacteria; ACY88167; ACY88167; STM14_1689.
DR   KEGG; seo:STM14_1689; -.
DR   PATRIC; fig|588858.6.peg.1624; -.
DR   HOGENOM; CLU_022474_4_0_6; -.
DR   OMA; MDNTTRF; -.
DR   BioCyc; SENT588858:STM14_RS07825-MON; -.
DR   Proteomes; UP000002695; Chromosome.
DR   GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0030257; C:type III protein secretion system complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0030254; P:protein secretion by the type III secretion system; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1370.120; -; 2.
DR   HAMAP; MF_02219; Type_III_secretin; 1.
DR   InterPro; IPR005644; NolW-like.
DR   InterPro; IPR038591; NolW-like_sf.
DR   InterPro; IPR004846; T2SS/T3SS.
DR   InterPro; IPR004845; T2SS_GspD_CS.
DR   InterPro; IPR003522; T3SS_OM_pore_YscC.
DR   Pfam; PF00263; Secretin; 1.
DR   Pfam; PF03958; Secretin_N; 1.
DR   PRINTS; PR01337; TYPE3OMGPROT.
DR   TIGRFAMs; TIGR02516; type_III_yscC; 1.
DR   PROSITE; PS00875; T2SP_D; 1.
PE   2: Evidence at transcript level;
KW   Cell outer membrane; Membrane; Protein transport; Signal; Translocation;
KW   Transport; Virulence.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT   CHAIN           21..497
FT                   /note="SPI-2 type 3 secretion system secretin"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02219"
FT                   /id="PRO_0000410497"
SQ   SEQUENCE   497 AA;  54113 MW;  B9E7E0B754A5DB31 CRC64;
     MVVNKRLILI LLFILNTAKS DELSWKGNDF TLYARQMPLA EVLHLLSENY DTAITISPLI
     TATFSGKIPP GPPVDILNNL AAQYDLLTWF DGSMLYVYPA SLLKHQVITF NILSTGRFIH
     YLRSQNILSS PGCEVKEITG TKAVEVSGVP SCLTRISQLA SVLDNALIKR KDSAVSVSIY
     TLKYATAMDT QYQYRDQSVV VPGVVSVLRE MSKTSVPTSS TNNGSPATQA LPMFAADPRQ
     NAVIVRDYAA NMAGYRKLIT ELDQRQQMIE ISVKIIDVNA GDINQLGIDW GTAVSLGGKK
     IAFNTGLNDG GASGFSTVIS DTSNFMVRLN ALEKSSQAYV LSQPSVVTLN NIQAVLDKNI
     TFYTKLQGEK VAKLESITTG SLLRVTPRLL NDNGTQKIML NLNIQDGQQS DTQSETDPLP
     EVQNSEIASQ ATLLAGQSLL LGGFKQGKQI HSQNKIPLLG DIPVVGHLFR NDTTQVHSVI
     RLFLIKASVV NNGISHG