INVA_YERPS
ID INVA_YERPS Reviewed; 985 AA.
AC P11922; Q66BU9;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 25-MAY-2022, entry version 136.
DE RecName: Full=Invasin;
GN OrderedLocusNames=YPTB1668;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3304658; DOI=10.1016/0092-8674(87)90335-7;
RA Isberg R.R., Voorhis D.L., Falkow S.;
RT "Identification of invasin: a protein that allows enteric bacteria to
RT penetrate cultured mammalian cells.";
RL Cell 50:769-778(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
RN [3]
RP DOMAIN INTEGRIN-BINDING.
RX PubMed=1693333; DOI=10.1002/j.1460-2075.1990.tb08326.x;
RA Leong J.M., Fournier R.S., Isberg R.R.;
RT "Identification of the integrin binding domain of the Yersinia
RT pseudotuberculosis invasin protein.";
RL EMBO J. 9:1979-1989(1990).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 494-985.
RX PubMed=10514372; DOI=10.1126/science.286.5438.291;
RA Hamburger Z.A., Brown M.S., Isberg R.R., Bjorkman P.J.;
RT "Crystal structure of invasin: a bacterial integrin-binding protein.";
RL Science 286:291-295(1999).
CC -!- FUNCTION: Invasin is a protein that allows enteric bacteria to
CC penetrate cultured mammalian cells. The entry of invasin in the cell is
CC mediated by binding several beta-1 chain integrins.
CC -!- SUBCELLULAR LOCATION: Cell surface.
CC -!- SIMILARITY: Belongs to the intimin/invasin family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1, Met-17 or Met-19 is the
CC initiator. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27632.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA27634.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA27635.1; Type=Erroneous initiation; 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; M17448; AAA27633.1; -; Genomic_DNA.
DR EMBL; M17448; AAA27632.1; ALT_INIT; Genomic_DNA.
DR EMBL; M17448; AAA27634.1; ALT_INIT; Genomic_DNA.
DR EMBL; M17448; AAA27635.1; ALT_INIT; Genomic_DNA.
DR EMBL; BX936398; CAH20907.1; -; Genomic_DNA.
DR PIR; A29646; A29646.
DR PDB; 1CWV; X-ray; 2.30 A; A=494-983.
DR PDB; 4E1T; X-ray; 2.26 A; A=147-390.
DR PDBsum; 1CWV; -.
DR PDBsum; 4E1T; -.
DR AlphaFoldDB; P11922; -.
DR SMR; P11922; -.
DR DrugBank; DB04272; Citric acid.
DR TCDB; 1.B.54.1.2; the intimin/invasin (int/inv) or autotransporter-3 (at-3) family.
DR EnsemblBacteria; CAH20907; CAH20907; YPTB1668.
DR KEGG; yps:YPTB1668; -.
DR OMA; GEYWVKK; -.
DR EvolutionaryTrace; P11922; -.
DR Proteomes; UP000001011; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.40.160.160; -; 1.
DR Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 3.10.100.10; -; 1.
DR InterPro; IPR003344; Big_1_dom.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR024519; IAT_beta.
DR InterPro; IPR038177; IAT_beta_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003535; Intimin/invasin_bac.
DR InterPro; IPR013117; Intimin_C.
DR InterPro; IPR008964; Invasin/intimin_cell_adhesion.
DR InterPro; IPR015217; Invasin_dom_3.
DR Pfam; PF02369; Big_1; 1.
DR Pfam; PF11924; IAT_beta; 1.
DR Pfam; PF07979; Intimin_C; 1.
DR Pfam; PF09134; Invasin_D3; 2.
DR PRINTS; PR01369; INTIMIN.
DR SMART; SM00634; BID_1; 3.
DR SUPFAM; SSF49373; SSF49373; 4.
DR SUPFAM; SSF56436; SSF56436; 1.
DR PROSITE; PS51127; BIG1; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Repeat.
FT CHAIN 1..985
FT /note="Invasin"
FT /id="PRO_0000211831"
FT TOPO_DOM 494..985
FT /note="Extracellular"
FT DOMAIN 503..594
FT /note="Big-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT DOMAIN 601..691
FT /note="Big-1 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00445"
FT REGION 494..594
FT /note="D1"
FT REGION 595..694
FT /note="D2"
FT REGION 695..794
FT /note="D3"
FT REGION 795..985
FT /note="Integrin-binding"
FT REGION 795..886
FT /note="D4"
FT REGION 887..985
FT /note="D5"
FT DISULFID 906..981
FT CONFLICT 767..768
FT /note="TA -> SV (in Ref. 1; AAA27633/AAA27632)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="T -> R (in Ref. 1; AAA27633/AAA27632)"
FT /evidence="ECO:0000305"
FT CONFLICT 970..971
FT /note="VQ -> QP (in Ref. 1; AAA27633/AAA27632)"
FT /evidence="ECO:0000305"
FT CONFLICT 984
FT /note="A -> S (in Ref. 1; AAA27633/AAA27632)"
FT /evidence="ECO:0000305"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 164..177
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 179..192
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 195..208
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 211..222
FT /evidence="ECO:0007829|PDB:4E1T"
FT TURN 223..226
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 227..238
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 241..250
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 270..279
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 282..294
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 312..323
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 326..334
FT /evidence="ECO:0007829|PDB:4E1T"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 340..351
FT /evidence="ECO:0007829|PDB:4E1T"
FT HELIX 356..359
FT /evidence="ECO:0007829|PDB:4E1T"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:4E1T"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:4E1T"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 387..390
FT /evidence="ECO:0007829|PDB:4E1T"
FT STRAND 503..510
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 512..519
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 521..528
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 539..543
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 552..556
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 561..568
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 573..581
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 584..593
FT /evidence="ECO:0007829|PDB:1CWV"
FT HELIX 599..601
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 603..613
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 619..624
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 638..647
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 654..663
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 668..676
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 679..691
FT /evidence="ECO:0007829|PDB:1CWV"
FT TURN 698..700
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 702..706
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 708..711
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 718..723
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 737..745
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 759..764
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 769..777
FT /evidence="ECO:0007829|PDB:1CWV"
FT HELIX 783..785
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 787..792
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 797..802
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 805..807
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 815..818
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 822..827
FT /evidence="ECO:0007829|PDB:1CWV"
FT HELIX 831..836
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 837..843
FT /evidence="ECO:0007829|PDB:1CWV"
FT TURN 844..846
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 847..849
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 854..857
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 865..874
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 878..883
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 887..892
FT /evidence="ECO:0007829|PDB:1CWV"
FT HELIX 899..905
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 912..914
FT /evidence="ECO:0007829|PDB:1CWV"
FT HELIX 917..920
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 926..929
FT /evidence="ECO:0007829|PDB:1CWV"
FT HELIX 931..935
FT /evidence="ECO:0007829|PDB:1CWV"
FT HELIX 938..940
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 947..957
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 959..963
FT /evidence="ECO:0007829|PDB:1CWV"
FT TURN 964..966
FT /evidence="ECO:0007829|PDB:1CWV"
FT STRAND 977..984
FT /evidence="ECO:0007829|PDB:1CWV"
SQ SEQUENCE 985 AA; 106544 MW; 42007F9EEB984D50 CRC64;
MVFQPISEFL LIRNAGMSMY FNKIISFNII SRIVICIFLI CGMFMAGASE KYDANAPQQV
QPYSVSSSAF ENLHPNNEME SSINPFSASD TERNAAIIDR ANKEQETEAV NKMISTGARL
AASGRASDVA HSMVGDAVNQ EIKQWLNRFG TAQVNLNFDK NFSLKESSLD WLAPWYDSAS
FLFFSQLGIR NKDSRNTLNL GVGIRTLENG WLYGLNTFYD NDLTGHNHRI GLGAEAWTDY
LQLAANGYFR LNGWHSSRDF SDYKERPATG GDLRANAYLP ALPQLGGKLM YEQYTGERVA
LFGKDNLQRN PYAVTAGINY TPVPLLTVGV DQRMGKSSKH ETQWNLQMNY RLGESFQSQL
SPSAVAGTRL LAESRYNLVD RNNNIVLEYQ KQQVVKLTLS PATISGLPGQ VYQVNAQVQG
ASAVREIVWS DAELIAAGGT LTPLSTTQFN LVLPPYKRTA QVSRVTDDLT ANFYSLSALA
VDHQGNRSNS FTLSVTVQQP QLTLTAAVIG DGAPANGKTA ITVEFTVADF EGKPLAGQEV
VITTNNGALP NKITEKTDAN GVARIALTNT TDGVTVVTAE VEGQRQSVDT HFVKGTIAAD
KSTLAAVPTS IIADGLMAST ITLELKDTYG DPQAGANVAF DTTLGNMGVI TDHNDGTYSA
PLTSTTLGVA TVTVKVDGAA FSVPSVTVNF TADPIPDAGR SSFTVSTPDI LADGTMSSTL
SFVPVDKNGH FISGMQGLSF TQNGVPVSIS PITEQPDSYT ATVVGNTAGD VTITPQVDTL
ILSTLQKKIS LFPVPTLTGI LVNGQNFATD KGFPKTIFKN ATFQLQMDND VANNTQYEWS
SSFTPNVSVN DQGQVTITYQ TYSEVAVTAK SKKFPSYSVS YRFYPNRWIY DGGTSLVSSL
EASRQCQGSD MSAVLESSRA TNGTRAPDGT LWGEWGSLTA YSSDWQSGEY WVKKTSTDFE
TMNMDTGALV QGPAYLAFPL CALAI
