SIPD_SALTY
ID SIPD_SALTY Reviewed; 343 AA.
AC Q56026; Q56033; Q7CPX2;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Cell invasion protein SipD;
DE AltName: Full=Salmonella invasion protein D;
GN Name=sipD; Synonyms=sspD; OrderedLocusNames=STM2883;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
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 [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SL1344;
RX PubMed=8522512; DOI=10.1128/jb.177.24.7078-7085.1995;
RA Kaniga K., Trollinger D., Galan J.E.;
RT "Identification of two targets of the type III protein secretion system
RT encoded by the inv and spa loci of Salmonella typhimurium that have
RT homology to the Shigella IpaD and IpaA proteins.";
RL J. Bacteriol. 177:7078-7085(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP FUNCTION.
RC STRAIN=SL1344;
RX PubMed=9194702; DOI=10.1046/j.1365-2958.1997.3781740.x;
RA Collazo C.M., Galan J.E.;
RT "The invasion-associated type III system of Salmonella typhimurium directs
RT the translocation of Sip proteins into the host cell.";
RL Mol. Microbiol. 24:747-756(1997).
RN [5]
RP REGULATION BY SICA AND INVF.
RC STRAIN=ATCC 14028s / SGSG 2262, LT2, and SL1344;
RX PubMed=10692170; DOI=10.1046/j.1365-2958.2000.01772.x;
RA Darwin K.H., Miller V.L.;
RT "The putative invasion protein chaperone SicA acts together with InvF to
RT activate the expression of Salmonella typhimurium virulence genes.";
RL Mol. Microbiol. 35:949-960(2000).
RN [6]
RP REGULATION BY INVE.
RX PubMed=12169593; DOI=10.1128/jb.184.17.4699-4708.2002;
RA Kubori T., Galan J.E.;
RT "Salmonella type III secretion-associated protein InvE controls
RT translocation of effector proteins into host cells.";
RL J. Bacteriol. 184:4699-4708(2002).
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. {ECO:0000269|PubMed:8522512,
CC ECO:0000269|PubMed:9194702}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8522512}.
CC Note=Secreted via the type III secretion system 1 (SPI-1 TTSS).
CC -!- INDUCTION: Transcriptionally regulated by SicA and InvF. Also regulated
CC by InvE.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA86617.1; Type=Frameshift; Evidence={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; U30491; AAC43548.1; -; Genomic_DNA.
DR EMBL; U40013; AAA86617.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE006468; AAL21763.1; -; Genomic_DNA.
DR PIR; S70549; S70549.
DR RefSeq; NP_461804.1; NC_003197.2.
DR RefSeq; WP_000932246.1; NC_003197.2.
DR PDB; 2YM0; X-ray; 3.00 A; A/B=132-343.
DR PDB; 2YM9; X-ray; 3.00 A; A/B/C/D=1-343.
DR PDB; 3NZZ; X-ray; 1.65 A; A/B=39-343.
DR PDB; 3O00; X-ray; 1.85 A; A/B=39-343.
DR PDB; 3O01; X-ray; 1.90 A; A/B=39-343.
DR PDB; 3O02; X-ray; 1.90 A; A/B=39-343.
DR PDB; 3ZQB; X-ray; 2.40 A; A/B=127-343.
DR PDB; 3ZQE; X-ray; 2.19 A; A/B=127-343.
DR PDBsum; 2YM0; -.
DR PDBsum; 2YM9; -.
DR PDBsum; 3NZZ; -.
DR PDBsum; 3O00; -.
DR PDBsum; 3O01; -.
DR PDBsum; 3O02; -.
DR PDBsum; 3ZQB; -.
DR PDBsum; 3ZQE; -.
DR AlphaFoldDB; Q56026; -.
DR BMRB; Q56026; -.
DR SMR; Q56026; -.
DR STRING; 99287.STM2883; -.
DR TCDB; 1.C.36.3.2; the bacterial type iii-target cell pore (iiitcp) family.
DR PaxDb; Q56026; -.
DR EnsemblBacteria; AAL21763; AAL21763; STM2883.
DR GeneID; 1254406; -.
DR KEGG; stm:STM2883; -.
DR PATRIC; fig|99287.12.peg.3039; -.
DR HOGENOM; CLU_069613_0_0_6; -.
DR OMA; NYLGVYE; -.
DR BioCyc; SENT99287:STM2883-MON; -.
DR EvolutionaryTrace; Q56026; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR DisProt; DP02796; -.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Reference proteome; Secreted; Virulence.
FT CHAIN 1..343
FT /note="Cell invasion protein SipD"
FT /id="PRO_0000219865"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 295..322
FT /evidence="ECO:0000255"
FT CONFLICT 292
FT /note="S -> A (in Ref. 2; AAA86617)"
FT /evidence="ECO:0000305"
FT HELIX 41..64
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 70..92
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:3NZZ"
FT TURN 115..117
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 150..171
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:3NZZ"
FT STRAND 178..180
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3ZQE"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 191..205
FT /evidence="ECO:0007829|PDB:3NZZ"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:3NZZ"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:3NZZ"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 228..238
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:3NZZ"
FT STRAND 245..248
FT /evidence="ECO:0007829|PDB:3NZZ"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 259..270
FT /evidence="ECO:0007829|PDB:3NZZ"
FT STRAND 275..278
FT /evidence="ECO:0007829|PDB:2YM9"
FT STRAND 280..283
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 284..338
FT /evidence="ECO:0007829|PDB:3NZZ"
FT HELIX 339..342
FT /evidence="ECO:0007829|PDB:2YM9"
SQ SEQUENCE 343 AA; 37112 MW; 4B8E46419114219F CRC64;
MLNIQNYSAS PHPGIVAERP QTPSASEHVE TAVVPSTTEH RGTDIISLSQ AATKIHQAQQ
TLQSTPPISE ENNDERTLAR QQLTSSLNAL AKSGVSLSAE QNENLRSAFS APTSALFSAS
PMAQPRTTIS DAEIWDMVSQ NISAIGDSYL GVYENVVAVY TDFYQAFSDI LSKMGGWLLP
GKDGNTVKLD VTSLKNDLNS LVNKYNQINS NTVLFPAQSG SGVKVATEAE ARQWLSELNL
PNSCLKSYGS GYVVTVDLTP LQKMVQDIDG LGAPGKDSKL EMDNAKYQAW QSGFKAQEEN
MKTTLQTLTQ KYSNANSLYD NLVKVLSSTI SSSLETAKSF LQG
