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Protein

Invasin

Gene

YPTB1668

Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Invasin is a protein that allows enteric bacteria to penetrate cultured mammalian cells. The entry of invasin in the cell is mediated by binding several beta-1 chain integrins.

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

BioCyciYPSE273123:GI1M-1743-MONOMER.

Protein family/group databases

TCDBi1.B.54.1.2. the intimin/invasin (int/inv) or autotransporter-3 (at-3) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Invasin
Gene namesi
Ordered Locus Names:YPTB1668
OrganismiYersinia pseudotuberculosis serotype I (strain IP32953)
Taxonomic identifieri273123 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia
Proteomesi
  • UP000001011 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini494 – 985492ExtracellularAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 985985InvasinPRO_0000211831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi906 ↔ 981

Keywords - PTMi

Disulfide bond

Structurei

Secondary structure

1
985
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi151 – 1588Combined sources
Beta strandi164 – 17714Combined sources
Beta strandi179 – 19214Combined sources
Beta strandi195 – 20814Combined sources
Beta strandi211 – 22212Combined sources
Turni223 – 2264Combined sources
Beta strandi227 – 23812Combined sources
Beta strandi241 – 25010Combined sources
Beta strandi264 – 2674Combined sources
Beta strandi270 – 27910Combined sources
Beta strandi282 – 29413Combined sources
Beta strandi296 – 2994Combined sources
Beta strandi308 – 3103Combined sources
Beta strandi312 – 32312Combined sources
Beta strandi326 – 3349Combined sources
Helixi336 – 3383Combined sources
Beta strandi340 – 35112Combined sources
Helixi356 – 3594Combined sources
Helixi362 – 3643Combined sources
Helixi365 – 3684Combined sources
Helixi371 – 3744Combined sources
Beta strandi387 – 3904Combined sources
Beta strandi503 – 5108Combined sources
Beta strandi512 – 5198Combined sources
Beta strandi521 – 5288Combined sources
Beta strandi539 – 5435Combined sources
Beta strandi552 – 5565Combined sources
Beta strandi561 – 5688Combined sources
Beta strandi573 – 5819Combined sources
Beta strandi584 – 59310Combined sources
Helixi599 – 6013Combined sources
Beta strandi603 – 61311Combined sources
Beta strandi619 – 6246Combined sources
Beta strandi638 – 64710Combined sources
Beta strandi654 – 66310Combined sources
Beta strandi668 – 6769Combined sources
Beta strandi679 – 69113Combined sources
Turni698 – 7003Combined sources
Beta strandi702 – 7065Combined sources
Beta strandi708 – 7114Combined sources
Beta strandi718 – 7236Combined sources
Beta strandi737 – 7459Combined sources
Beta strandi759 – 7646Combined sources
Beta strandi769 – 7779Combined sources
Helixi783 – 7853Combined sources
Beta strandi787 – 7926Combined sources
Beta strandi797 – 8026Combined sources
Beta strandi805 – 8073Combined sources
Beta strandi815 – 8184Combined sources
Beta strandi822 – 8276Combined sources
Helixi831 – 8366Combined sources
Beta strandi837 – 8437Combined sources
Turni844 – 8463Combined sources
Beta strandi847 – 8493Combined sources
Beta strandi854 – 8574Combined sources
Beta strandi865 – 87410Combined sources
Beta strandi878 – 8836Combined sources
Beta strandi887 – 8926Combined sources
Helixi899 – 9057Combined sources
Beta strandi912 – 9143Combined sources
Helixi917 – 9204Combined sources
Beta strandi926 – 9294Combined sources
Helixi931 – 9355Combined sources
Helixi938 – 9403Combined sources
Beta strandi947 – 95711Combined sources
Beta strandi959 – 9635Combined sources
Turni964 – 9663Combined sources
Beta strandi977 – 9837Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWVX-ray2.30A494-983[»]
4E1TX-ray2.26A147-390[»]
ProteinModelPortaliP11922.
SMRiP11922. Positions 502-985.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP11922.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini503 – 59492Big-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini601 – 69191Big-1 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni494 – 594101D1Add
BLAST
Regioni595 – 694100D2Add
BLAST
Regioni695 – 794100D3Add
BLAST
Regioni795 – 985191Integrin-bindingAdd
BLAST
Regioni795 – 88692D4Add
BLAST
Regioni887 – 98599D5Add
BLAST

Sequence similaritiesi

Belongs to the intimin/invasin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000219559.
OMAiFETMNMD.
OrthoDBiEOG6M9DRK.

Family and domain databases

Gene3Di2.60.40.920. 3 hits.
3.10.100.10. 1 hit.
InterProiIPR003344. Big_1_dom.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR003535. Intimin/invasin_bac.
IPR013117. Intimin_C.
IPR008964. Invasin/intimin_cell_adhesion.
IPR024519. Invasin_beta.
IPR015217. Invasin_dom_3.
[Graphical view]
PfamiPF02369. Big_1. 1 hit.
PF07979. Intimin_C. 1 hit.
PF11924. Invasin_beta. 1 hit.
PF09134. Invasin_D3. 2 hits.
[Graphical view]
PRINTSiPR01369. INTIMIN.
SMARTiSM00634. BID_1. 3 hits.
[Graphical view]
SUPFAMiSSF49373. SSF49373. 4 hits.
SSF56436. SSF56436. 1 hit.
PROSITEiPS51127. BIG1. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P11922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVFQPISEFL LIRNAGMSMY FNKIISFNII SRIVICIFLI CGMFMAGASE
60 70 80 90 100
KYDANAPQQV QPYSVSSSAF ENLHPNNEME SSINPFSASD TERNAAIIDR
110 120 130 140 150
ANKEQETEAV NKMISTGARL AASGRASDVA HSMVGDAVNQ EIKQWLNRFG
160 170 180 190 200
TAQVNLNFDK NFSLKESSLD WLAPWYDSAS FLFFSQLGIR NKDSRNTLNL
210 220 230 240 250
GVGIRTLENG WLYGLNTFYD NDLTGHNHRI GLGAEAWTDY LQLAANGYFR
260 270 280 290 300
LNGWHSSRDF SDYKERPATG GDLRANAYLP ALPQLGGKLM YEQYTGERVA
310 320 330 340 350
LFGKDNLQRN PYAVTAGINY TPVPLLTVGV DQRMGKSSKH ETQWNLQMNY
360 370 380 390 400
RLGESFQSQL SPSAVAGTRL LAESRYNLVD RNNNIVLEYQ KQQVVKLTLS
410 420 430 440 450
PATISGLPGQ VYQVNAQVQG ASAVREIVWS DAELIAAGGT LTPLSTTQFN
460 470 480 490 500
LVLPPYKRTA QVSRVTDDLT ANFYSLSALA VDHQGNRSNS FTLSVTVQQP
510 520 530 540 550
QLTLTAAVIG DGAPANGKTA ITVEFTVADF EGKPLAGQEV VITTNNGALP
560 570 580 590 600
NKITEKTDAN GVARIALTNT TDGVTVVTAE VEGQRQSVDT HFVKGTIAAD
610 620 630 640 650
KSTLAAVPTS IIADGLMAST ITLELKDTYG DPQAGANVAF DTTLGNMGVI
660 670 680 690 700
TDHNDGTYSA PLTSTTLGVA TVTVKVDGAA FSVPSVTVNF TADPIPDAGR
710 720 730 740 750
SSFTVSTPDI LADGTMSSTL SFVPVDKNGH FISGMQGLSF TQNGVPVSIS
760 770 780 790 800
PITEQPDSYT ATVVGNTAGD VTITPQVDTL ILSTLQKKIS LFPVPTLTGI
810 820 830 840 850
LVNGQNFATD KGFPKTIFKN ATFQLQMDND VANNTQYEWS SSFTPNVSVN
860 870 880 890 900
DQGQVTITYQ TYSEVAVTAK SKKFPSYSVS YRFYPNRWIY DGGTSLVSSL
910 920 930 940 950
EASRQCQGSD MSAVLESSRA TNGTRAPDGT LWGEWGSLTA YSSDWQSGEY
960 970 980
WVKKTSTDFE TMNMDTGALV QGPAYLAFPL CALAI
Length:985
Mass (Da):106,544
Last modified:November 23, 2004 - v2
Checksum:i42007F9EEB984D50
GO

Sequence cautioni

The sequence AAA27632.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA27634.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAA27635.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti767 – 7682TA → SV in AAA27633 (PubMed:3304658).Curated
Sequence conflicti767 – 7682TA → SV in AAA27632 (PubMed:3304658).Curated
Sequence conflicti894 – 8941T → R in AAA27633 (PubMed:3304658).Curated
Sequence conflicti894 – 8941T → R in AAA27632 (PubMed:3304658).Curated
Sequence conflicti970 – 9712VQ → QP in AAA27633 (PubMed:3304658).Curated
Sequence conflicti970 – 9712VQ → QP in AAA27632 (PubMed:3304658).Curated
Sequence conflicti984 – 9841A → S in AAA27633 (PubMed:3304658).Curated
Sequence conflicti984 – 9841A → S in AAA27632 (PubMed:3304658).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17448 Genomic DNA. Translation: AAA27633.1.
M17448 Genomic DNA. Translation: AAA27632.1. Different initiation.
M17448 Genomic DNA. Translation: AAA27634.1. Different initiation.
M17448 Genomic DNA. Translation: AAA27635.1. Different initiation.
BX936398 Genomic DNA. Translation: CAH20907.1.
PIRiA29646.

Genome annotation databases

EnsemblBacteriaiCAH20907; CAH20907; YPTB1668.
KEGGiyps:YPTB1668.
PATRICi18642013. VBIYerPse22266_2071.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M17448 Genomic DNA. Translation: AAA27633.1.
M17448 Genomic DNA. Translation: AAA27632.1. Different initiation.
M17448 Genomic DNA. Translation: AAA27634.1. Different initiation.
M17448 Genomic DNA. Translation: AAA27635.1. Different initiation.
BX936398 Genomic DNA. Translation: CAH20907.1.
PIRiA29646.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1CWVX-ray2.30A494-983[»]
4E1TX-ray2.26A147-390[»]
ProteinModelPortaliP11922.
SMRiP11922. Positions 502-985.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

TCDBi1.B.54.1.2. the intimin/invasin (int/inv) or autotransporter-3 (at-3) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH20907; CAH20907; YPTB1668.
KEGGiyps:YPTB1668.
PATRICi18642013. VBIYerPse22266_2071.

Phylogenomic databases

HOGENOMiHOG000219559.
OMAiFETMNMD.
OrthoDBiEOG6M9DRK.

Enzyme and pathway databases

BioCyciYPSE273123:GI1M-1743-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP11922.

Family and domain databases

Gene3Di2.60.40.920. 3 hits.
3.10.100.10. 1 hit.
InterProiIPR003344. Big_1_dom.
IPR016186. C-type_lectin-like.
IPR016187. C-type_lectin_fold.
IPR003535. Intimin/invasin_bac.
IPR013117. Intimin_C.
IPR008964. Invasin/intimin_cell_adhesion.
IPR024519. Invasin_beta.
IPR015217. Invasin_dom_3.
[Graphical view]
PfamiPF02369. Big_1. 1 hit.
PF07979. Intimin_C. 1 hit.
PF11924. Invasin_beta. 1 hit.
PF09134. Invasin_D3. 2 hits.
[Graphical view]
PRINTSiPR01369. INTIMIN.
SMARTiSM00634. BID_1. 3 hits.
[Graphical view]
SUPFAMiSSF49373. SSF49373. 4 hits.
SSF56436. SSF56436. 1 hit.
PROSITEiPS51127. BIG1. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of invasin: a protein that allows enteric bacteria to penetrate cultured mammalian cells."
    Isberg R.R., Voorhis D.L., Falkow S.
    Cell 50:769-778(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: IP32953.
  3. "Identification of the integrin binding domain of the Yersinia pseudotuberculosis invasin protein."
    Leong J.M., Fournier R.S., Isberg R.R.
    EMBO J. 9:1979-1989(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN INTEGRIN-BINDING.
  4. "Crystal structure of invasin: a bacterial integrin-binding protein."
    Hamburger Z.A., Brown M.S., Isberg R.R., Bjorkman P.J.
    Science 286:291-295(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 494-985.

Entry informationi

Entry nameiINVA_YERPS
AccessioniPrimary (citable) accession number: P11922
Secondary accession number(s): Q66BU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: November 23, 2004
Last modified: May 11, 2016
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Caution

It is uncertain whether Met-1, Met-17 or Met-19 is the initiator.Curated

Keywords - Technical termi

3D-structure, Complete 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.