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Protein

Cell invasion protein SipD

Gene

sipD

Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Required for translocation of effector proteins via the type III secretion system SPI-1, which is essential for an efficient bacterial internalization. Probably acts by modulating the secretion of SipA, SipB, and SipC.2 Publications

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Virulence

Protein family/group databases

TCDBi1.C.36.3.2. the bacterial type iii-target cell pore (iiitcp) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cell invasion protein SipD
Alternative name(s):
Salmonella invasion protein D
Gene namesi
Name:sipD
Synonyms:sspD
Ordered Locus Names:STM2883
OrganismiSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Taxonomic identifieri99287 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeSalmonella
Proteomesi
  • UP000001014 Componenti: Chromosome

Subcellular locationi

  • Secreted 1 Publication

  • Note: Secreted via the type III secretion system 1 (SPI-1 TTSS).

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002198651 – 343Cell invasion protein SipDAdd BLAST343

Proteomic databases

PaxDbiQ56026.
PRIDEiQ56026.

Expressioni

Inductioni

Transcriptionally regulated by SicA and InvF. Also regulated by InvE.

Interactioni

Protein-protein interaction databases

STRINGi99287.STM2883.

Structurei

Secondary structure

1343
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi41 – 64Combined sources24
Helixi70 – 92Combined sources23
Helixi99 – 108Combined sources10
Turni115 – 117Combined sources3
Helixi133 – 148Combined sources16
Helixi150 – 171Combined sources22
Helixi172 – 177Combined sources6
Beta strandi178 – 180Combined sources3
Helixi182 – 184Combined sources3
Beta strandi186 – 189Combined sources4
Helixi191 – 205Combined sources15
Turni210 – 212Combined sources3
Beta strandi213 – 216Combined sources4
Beta strandi220 – 222Combined sources3
Helixi228 – 238Combined sources11
Helixi242 – 244Combined sources3
Beta strandi245 – 248Combined sources4
Beta strandi251 – 255Combined sources5
Helixi259 – 270Combined sources12
Beta strandi275 – 278Combined sources4
Beta strandi280 – 283Combined sources4
Helixi284 – 338Combined sources55
Helixi339 – 342Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YM0X-ray3.00A/B132-343[»]
2YM9X-ray3.00A/B/C/D1-343[»]
3NZZX-ray1.65A/B39-343[»]
3O00X-ray1.85A/B39-343[»]
3O01X-ray1.90A/B39-343[»]
3O02X-ray1.90A/B39-343[»]
3ZQBX-ray2.40A/B127-343[»]
3ZQEX-ray2.19A/B127-343[»]
ProteinModelPortaliQ56026.
SMRiQ56026.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ56026.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili295 – 322Sequence analysisAdd BLAST28

Domaini

The N-terminal domain is an intra-molecular chaperone that prevents premature oligomerization of the residues on the coiled-coil region that are involved in interactions with the needle and/or itself. The residues in the C-terminal domain probably form oligomeric structures at the tip of the needle that are responsible for the regulation of secretion of other effectors (By similarity).By similarity

Sequence similaritiesi

Belongs to the invasin protein D family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG4105IBT. Bacteria.
ENOG4111P3X. LUCA.
HOGENOMiHOG000028233.
KOiK13287.
OMAiNYLGVYE.

Family and domain databases

InterProiIPR009483. Plasmid_invsIpaD.
IPR013386. T3SS_IpaD/SipD/SspD.
[Graphical view]
PfamiPF06511. IpaD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02553. SipD_IpaD_SspD. 1 hit.

Sequencei

Sequence statusi: Complete.

Q56026-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLNIQNYSAS PHPGIVAERP QTPSASEHVE TAVVPSTTEH RGTDIISLSQ
60 70 80 90 100
AATKIHQAQQ TLQSTPPISE ENNDERTLAR QQLTSSLNAL AKSGVSLSAE
110 120 130 140 150
QNENLRSAFS APTSALFSAS PMAQPRTTIS DAEIWDMVSQ NISAIGDSYL
160 170 180 190 200
GVYENVVAVY TDFYQAFSDI LSKMGGWLLP GKDGNTVKLD VTSLKNDLNS
210 220 230 240 250
LVNKYNQINS NTVLFPAQSG SGVKVATEAE ARQWLSELNL PNSCLKSYGS
260 270 280 290 300
GYVVTVDLTP LQKMVQDIDG LGAPGKDSKL EMDNAKYQAW QSGFKAQEEN
310 320 330 340
MKTTLQTLTQ KYSNANSLYD NLVKVLSSTI SSSLETAKSF LQG
Length:343
Mass (Da):37,112
Last modified:November 1, 1996 - v1
Checksum:i4B8E46419114219F
GO

Sequence cautioni

The sequence AAA86617 differs from that shown. Reason: Frameshift at position 333.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti292S → A in AAA86617 (PubMed:8522512).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30491 Genomic DNA. Translation: AAC43548.1.
U40013 Genomic DNA. Translation: AAA86617.1. Frameshift.
AE006468 Genomic DNA. Translation: AAL21763.1.
PIRiS70549.
RefSeqiNP_461804.1. NC_003197.1.
WP_000932246.1. NC_003197.1.

Genome annotation databases

EnsemblBacteriaiAAL21763; AAL21763; STM2883.
GeneIDi1254406.
KEGGistm:STM2883.
PATRICi32384454. VBISalEnt20916_3039.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U30491 Genomic DNA. Translation: AAC43548.1.
U40013 Genomic DNA. Translation: AAA86617.1. Frameshift.
AE006468 Genomic DNA. Translation: AAL21763.1.
PIRiS70549.
RefSeqiNP_461804.1. NC_003197.1.
WP_000932246.1. NC_003197.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YM0X-ray3.00A/B132-343[»]
2YM9X-ray3.00A/B/C/D1-343[»]
3NZZX-ray1.65A/B39-343[»]
3O00X-ray1.85A/B39-343[»]
3O01X-ray1.90A/B39-343[»]
3O02X-ray1.90A/B39-343[»]
3ZQBX-ray2.40A/B127-343[»]
3ZQEX-ray2.19A/B127-343[»]
ProteinModelPortaliQ56026.
SMRiQ56026.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi99287.STM2883.

Protein family/group databases

TCDBi1.C.36.3.2. the bacterial type iii-target cell pore (iiitcp) family.

Proteomic databases

PaxDbiQ56026.
PRIDEiQ56026.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL21763; AAL21763; STM2883.
GeneIDi1254406.
KEGGistm:STM2883.
PATRICi32384454. VBISalEnt20916_3039.

Phylogenomic databases

eggNOGiENOG4105IBT. Bacteria.
ENOG4111P3X. LUCA.
HOGENOMiHOG000028233.
KOiK13287.
OMAiNYLGVYE.

Miscellaneous databases

EvolutionaryTraceiQ56026.

Family and domain databases

InterProiIPR009483. Plasmid_invsIpaD.
IPR013386. T3SS_IpaD/SipD/SspD.
[Graphical view]
PfamiPF06511. IpaD. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02553. SipD_IpaD_SspD. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSIPD_SALTY
AccessioniPrimary (citable) accession number: Q56026
Secondary accession number(s): Q56033, Q7CPX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.