ID   SIPD_SALPA              Reviewed;         340 AA.
AC   Q5PEC2;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Cell invasion protein SipD;
DE   AltName: Full=Salmonella invasion protein D;
GN   Name=sipD; Synonyms=sspD; OrderedLocusNames=SPA2741;
OS   Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=295319;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9150 / SARB42;
RX   PubMed=15531882; DOI=10.1038/ng1470;
RA   McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA   Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA   Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA   Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA   Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA   Warren W., Florea L., Spieth J., Wilson R.K.;
RT   "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT   restricted serovars of Salmonella enterica that cause typhoid.";
RL   Nat. Genet. 36:1268-1274(2004).
CC   -!- FUNCTION: Required for translocation of effector proteins via the type
CC       III secretion system SPI-1, which is essential for an efficient
CC       bacterial internalization. Probably acts by modulating the secretion of
CC       SipA, SipB, and SipC (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted via the
CC       type III secretion system 1 (SPI-1 TTSS). Localizes to the tip of the
CC       external secretion needle that is part of the TTSS apparatus (By
CC       similarity). {ECO:0000250}.
CC   -!- INDUCTION: Transcriptionally regulated by SicA and InvF. Also regulated
CC       by InvE (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain is an intra-molecular chaperone that
CC       prevents premature oligomerization of the residues on the coiled-coil
CC       region that are involved in interactions with the needle and/or itself.
CC       The residues in the C-terminal domain probably form oligomeric
CC       structures at the tip of the needle that are responsible for the
CC       regulation of secretion of other effectors (By similarity).
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the invasin protein D family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000026; AAV78598.1; -; Genomic_DNA.
DR   RefSeq; WP_000932243.1; NC_006511.1.
DR   AlphaFoldDB; Q5PEC2; -.
DR   SMR; Q5PEC2; -.
DR   EnsemblBacteria; AAV78598; AAV78598; SPA2741.
DR   KEGG; spt:SPA2741; -.
DR   HOGENOM; CLU_069613_0_0_6; -.
DR   OMA; NYLGVYE; -.
DR   Proteomes; UP000008185; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   Gene3D; 1.20.1710.10; -; 1.
DR   InterPro; IPR036708; BipD-like_sf.
DR   InterPro; IPR009483; IpaD.
DR   Pfam; PF06511; T3SS_TC; 1.
DR   SUPFAM; SSF140693; SSF140693; 1.
DR   TIGRFAMs; TIGR02553; SipD_IpaD_SspD; 1.
PE   3: Inferred from homology;
KW   Coiled coil; Secreted; Virulence.
FT   CHAIN           1..340
FT                   /note="Cell invasion protein SipD"
FT                   /id="PRO_0000219863"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          57..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          291..319
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   340 AA;  36549 MW;  425378F6CC254D3C CRC64;
     MLNIQNYSAS PHPGIVAERP QTPSASEHAE IAVVPSTTEH RGTDIISLSQ AATKIQQAQQ
     TLQSTPPISE ENNDERTLAR QQLTSSLNAL AKSGVSLSAE QNENLRSTFS APTSALFSAS
     PMAQPRTTIS DAEIWDMVSQ NISAIGDSYL GVYENVVAVY TDFYQAFSDI LSKMGGWLSP
     GKDGNTIKLN VDSLKSEISS LINKYTQINK NTILFPSQTG SGMTTATKAE AEQWIKELNL
     PDSCLKASGS GYVVLVDTGP LSKMVSDLNG IGSGSALELD NAKYQAWQSG FKAQEENLKT
     TLQTLTQKYS NANSLYDNLV KVLSSTISSS LETAKSFLQG