INLA_LISMO
ID INLA_LISMO Reviewed; 800 AA.
AC P0DJM0; P25146; Q45GD5; Q45GD6; Q48748; Q48749; Q48750; Q48752; Q9EXG2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2012, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Internalin A {ECO:0000303|PubMed:1905979};
DE Flags: Precursor;
GN Name=inlA {ECO:0000303|PubMed:1905979}; OrderedLocusNames=lmo0433;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DOMAIN, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=EGD-SmR / Serovar 1/2a;
RX PubMed=1905979; DOI=10.1016/0092-8674(91)90009-n;
RA Gaillard J.-L., Berche P., Frehel C., Gouin E., Cossart P.;
RT "Entry of L. monocytogenes into cells is mediated by internalin, a repeat
RT protein reminiscent of surface antigens from Gram-positive cocci.";
RL Cell 65:1127-1141(1991).
RN [2]
RP SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=EGD-SmR / Serovar 1/2a;
RX PubMed=7934917; DOI=10.1111/j.1365-2958.1993.tb01241.x;
RA Dramsi S., Dehoux P., Cossart P.;
RT "Common features of Gram-positive bacterial proteins involved in cell
RT recognition.";
RL Mol. Microbiol. 9:1119-1121(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=EGD / Mackaness / Serovar 1/2a;
RA Hain T., Pashalidis P., Hudel M., Chakraborty T., Domann E.;
RT "Nucleotide sequence of the internalin operon from Listeria monocytogenes
RT EGD.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=H4;
RA Jiang L., Xu J., Chen N., Chen X., Fang W.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [6]
RP PROTEIN SEQUENCE OF 36-40, SUBCELLULAR LOCATION, AND PROCESSING BY SRTA.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11854224; DOI=10.1128/iai.70.3.1382-1390.2002;
RA Garandeau C., Reglier-Poupet H., Dubail I., Beretti J.L., Berche P.,
RA Charbit A.;
RT "The sortase SrtA of Listeria monocytogenes is involved in processing of
RT internalin and in virulence.";
RL Infect. Immun. 70:1382-1390(2002).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-418.
RC STRAIN=F4233 / Serotype 1/2b, F5782 / Serotype 4b, and
RC F6789 / Serotype 1/2b;
RX PubMed=9541569; DOI=10.1007/s002849900315;
RA Vines A., Swaminathan B.;
RT "Identification and characterization of nucleotide sequence differences in
RT three virulence-associated genes of Listeria monocytogenes strains
RT representing clinically important serotypes.";
RL Curr. Microbiol. 36:309-318(1998).
RN [8]
RP PROTEIN SEQUENCE OF 764-770, SUBCELLULAR LOCATION, SORTING SIGNAL, AND CELL
RP WALL ANCHORING.
RC STRAIN=EGD / Mackaness / Serovar 1/2a;
RX PubMed=10736172; DOI=10.1021/bi992347o;
RA Dhar G., Faull K.F., Schneewind O.;
RT "Anchor structure of cell wall surface proteins in Listeria
RT monocytogenes.";
RL Biochemistry 39:3725-3733(2000).
RN [9]
RP IDENTIFICATION OF HOST RECEPTOR, FUNCTION, ACTIVITY REGULATION, INTERACTION
RP WITH HUMAN CDH1, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=8601315; DOI=10.1016/s0092-8674(00)81070-3;
RA Mengaud J., Ohayon H., Gounon P., Mege R.M., Cossart P.;
RT "E-cadherin is the receptor for internalin, a surface protein required for
RT entry of L. monocytogenes into epithelial cells.";
RL Cell 84:923-932(1996).
RN [10]
RP FUNCTION, HOST SPECIFICITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=10406800; DOI=10.1093/emboj/18.14.3956;
RA Lecuit M., Dramsi S., Gottardi C., Fedor-Chaiken M., Gumbiner B.,
RA Cossart P.;
RT "A single amino acid in E-cadherin responsible for host specificity towards
RT the human pathogen Listeria monocytogenes.";
RL EMBO J. 18:3956-3963(1999).
RN [11]
RP PROCESSING BY SRTA, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11929538; DOI=10.1046/j.1365-2958.2002.02798.x;
RA Bierne H., Mazmanian S.K., Trost M., Pucciarelli M.G., Liu G., Dehoux P.,
RA Jansch L., Garcia-del Portillo F., Schneewind O., Cossart P.;
RT "Inactivation of the srtA gene in Listeria monocytogenes inhibits anchoring
RT of surface proteins and affects virulence.";
RL Mol. Microbiol. 43:869-881(2002).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND PROCESSING BY SRTA.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=16247833; DOI=10.1002/pmic.200402075;
RA Pucciarelli M.G., Calvo E., Sabet C., Bierne H., Cossart P.,
RA Garcia-del Portillo F.;
RT "Identification of substrates of the Listeria monocytogenes sortases A and
RT B by a non-gel proteomic analysis.";
RL Proteomics 5:4808-4817(2005).
RN [13]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=20176794; DOI=10.1128/iai.01096-09;
RA Personnic N., Bruck S., Nahori M.A., Toledo-Arana A., Nikitas G.,
RA Lecuit M., Dussurget O., Cossart P., Bierne H.;
RT "The stress-induced virulence protein InlH controls interleukin-6
RT production during murine listeriosis.";
RL Infect. Immun. 78:1979-1989(2010).
RN [14]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=21725001; DOI=10.1128/jb.01154-10;
RA Bruck S., Personnic N., Prevost M.C., Cossart P., Bierne H.;
RT "Regulated shift from helical to polar localization of Listeria
RT monocytogenes cell wall-anchored proteins.";
RL J. Bacteriol. 193:4425-4437(2011).
RN [15]
RP SUBCELLULAR LOCATION, AND PROCESSING BY SRTA.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=22837151; DOI=10.2436/20.1501.01.157;
RA Mariscotti J.F., Quereda J.J., Pucciarelli M.G.;
RT "Contribution of sortase A to the regulation of Listeria monocytogenes
RT LPXTG surface proteins.";
RL Int. Microbiol. 15:43-51(2012).
RN [16] {ECO:0007744|PDB:1O6S, ECO:0007744|PDB:1O6T, ECO:0007744|PDB:1O6V}
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 36-496 ALONE AND IN COMPLEX WITH
RP HUMAN CDH1, SUBUNIT, DOMAIN, AND MUTAGENESIS OF PHE-150; TYR-343; TYR-347;
RP PHE-367; TYR-369 AND TRP-387.
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=12526809; DOI=10.1016/s0092-8674(02)01136-4;
RA Schubert W.-D., Urbanke C., Ziehm T., Beier V., Machner M.P., Domann E.,
RA Wehland J., Chakraborty T., Heinz D.W.;
RT "Structure of internalin, a major invasion protein of Listeria
RT monocytogenes, in complex with its human receptor E-cadherin.";
RL Cell 111:825-836(2002).
RN [17] {ECO:0007744|PDB:2OMV, ECO:0007744|PDB:2OMW, ECO:0007744|PDB:2OMY}
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 36-495 IN COMPLEX WITH HUMAN OR
RP MOUSE CDH1, SUBUNIT, DOMAIN, AND MUTAGENESIS OF SER-192 AND TYR-369.
RX PubMed=17540170; DOI=10.1016/j.cell.2007.03.049;
RA Wollert T., Pasche B., Rochon M., Deppenmeier S., van den Heuvel J.,
RA Gruber A.D., Heinz D.W., Lengeling A., Schubert W.D.;
RT "Extending the host range of Listeria monocytogenes by rational protein
RT design.";
RL Cell 129:891-902(2007).
RN [18] {ECO:0007744|PDB:2OMT, ECO:0007744|PDB:2OMU, ECO:0007744|PDB:2OMX, ECO:0007744|PDB:2OMZ}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 36-495 IN COMPLEX WITH HUMAN
RP CDH1, SUBUNIT, DOMAIN, AND MUTAGENESIS OF SER-192; GLY-194 AND TYR-369.
RX PubMed=17715295; DOI=10.1073/pnas.0702199104;
RA Wollert T., Heinz D.W., Schubert W.D.;
RT "Thermodynamically reengineering the listerial invasion complex InlA/E-
RT cadherin.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:13960-13965(2007).
CC -!- FUNCTION: Mediates the entry of L.monocytogenes into host intestinal
CC epithelial cells; transformation with inlA alone allows L.innocua (a
CC non-invasive species) to be taken up by host cells (PubMed:1905979,
CC PubMed:8601315, PubMed:10406800). Binds to human receptor cadherin-1
CC (E-cadherin, CDH1); the chicken homolog of cadherin-1 but not cadherin-
CC 2 function as receptors (PubMed:8601315). Mouse cadherin-1 is not a
CC receptor, however mutating a single surface-exposed residue (Glu-172 to
CC Pro in mouse) allows cadherin-1 to act as a receptor for InlA
CC (PubMed:10406800). {ECO:0000269|PubMed:10406800,
CC ECO:0000269|PubMed:1905979, ECO:0000269|PubMed:8601315}.
CC -!- ACTIVITY REGULATION: Bacterial uptake is inhibited by EDTA and by anti-
CC E-cadherin antibodies. {ECO:0000269|PubMed:8601315}.
CC -!- SUBUNIT: Interacts with host (human) cadherin-1 (CDH1)
CC (PubMed:12526809, PubMed:17540170, PubMed:17715295). The formation of
CC the complex between inlA and cadherin-1 is calcium-dependent
CC (PubMed:12526809). Mutagenesis studies show it is possible to increase
CC the affinity of InlA for CDH1 by rational engineering of InlA residues
CC (PubMed:17715295). {ECO:0000269|PubMed:12526809,
CC ECO:0000269|PubMed:17540170, ECO:0000269|PubMed:17715295}.
CC -!- INTERACTION:
CC P0DJM0; P12830: CDH1; Xeno; NbExp=3; IntAct=EBI-1035388, EBI-727477;
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-
CC ProRule:PRU00477, ECO:0000269|PubMed:10736172,
CC ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:20176794,
CC ECO:0000269|PubMed:21725001, ECO:0000269|PubMed:22837151};
CC Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477,
CC ECO:0000269|PubMed:10736172, ECO:0000269|PubMed:11929538}. Secreted
CC {ECO:0000269|PubMed:11854224, ECO:0000269|PubMed:20176794}. Note=In the
CC absence of SrtA in exponential phase some protein is still anchored to
CC the cell wall and a very small amount is secreted while overall protein
CC levels are the same in the srtA mutant; in stationary phase almost no
CC protein accumulates (PubMed:22837151). During exponential growth
CC detected on the cell surface as a series of dots in a helical pattern,
CC it is excluded from the septum; if expression is increased it
CC accumulates at cell poles (PubMed:21725001). The helical pattern of
CC InlA does not overlap with that of InlH, InlJ or Hbp2 (SvpA)
CC (PubMed:21725001). In stationary phase colocalizes with InlH at cell
CC poles and at the septum, the location shift requires SigB
CC (PubMed:21725001). {ECO:0000269|PubMed:21725001,
CC ECO:0000269|PubMed:22837151}.
CC -!- INDUCTION: More prevalent in stationary than exponential phase (at
CC protein level) (PubMed:16247833, PubMed:21725001). Levels maybe post-
CC transcriptionally decreased by InlH; disruption of inlH in some strains
CC (EGD-e and EGD-2) leads to increased levels of InlA (at protein level)
CC (PubMed:20176794). {ECO:0000269|PubMed:16247833,
CC ECO:0000269|PubMed:20176794, ECO:0000269|PubMed:21725001}.
CC -!- DOMAIN: Consists of an N-terminal cap, a leucine-rich repeat domain
CC (LRR), and an Ig-like interrepeat domain. {ECO:0000269|PubMed:12526809,
CC ECO:0000269|PubMed:17540170, ECO:0000269|PubMed:17715295}.
CC -!- DISRUPTION PHENOTYPE: Deletion of both inlA and inlB prevents bacterial
CC uptake by human enterocyte-like cell line Caco-2 (PubMed:1905979).
CC Deletion of inlA alone decreases host cell entry; the reduction varies
CC from 98% to none depending on the cell line tested (PubMed:11929538,
CC PubMed:8601315, PubMed:10406800). {ECO:0000269|PubMed:10406800,
CC ECO:0000269|PubMed:11929538, ECO:0000269|PubMed:1905979,
CC ECO:0000269|PubMed:8601315}.
CC -!- SIMILARITY: Belongs to the internalin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA25289.1; Type=Frameshift; Evidence={ECO:0000305|PubMed:7934917};
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DR EMBL; M67471; AAA25289.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AJ012346; CAC20628.1; -; Genomic_DNA.
DR EMBL; DQ132794; AAZ53235.1; -; Genomic_DNA.
DR EMBL; AL591975; CAC98512.1; -; Genomic_DNA.
DR EMBL; U25448; AAA69530.1; -; Genomic_DNA.
DR EMBL; U25451; AAA69533.1; -; Genomic_DNA.
DR EMBL; U25454; AAA69536.1; -; Genomic_DNA.
DR PIR; AB1129; AB1129.
DR RefSeq; NP_463962.1; NC_003210.1.
DR RefSeq; WP_010989462.1; NZ_CP023861.1.
DR PDB; 1O6S; X-ray; 1.80 A; A=36-496.
DR PDB; 1O6T; X-ray; 1.60 A; A=36-496.
DR PDB; 1O6V; X-ray; 1.50 A; A/B=36-496.
DR PDB; 2OMT; X-ray; 2.00 A; A=36-496.
DR PDB; 2OMU; X-ray; 1.80 A; A=36-496.
DR PDB; 2OMV; X-ray; 1.90 A; A=36-495.
DR PDB; 2OMW; X-ray; 1.85 A; A=36-496.
DR PDB; 2OMX; X-ray; 1.70 A; A=36-496.
DR PDB; 2OMY; X-ray; 1.70 A; A=36-495.
DR PDB; 2OMZ; X-ray; 1.60 A; A=36-495.
DR PDBsum; 1O6S; -.
DR PDBsum; 1O6T; -.
DR PDBsum; 1O6V; -.
DR PDBsum; 2OMT; -.
DR PDBsum; 2OMU; -.
DR PDBsum; 2OMV; -.
DR PDBsum; 2OMW; -.
DR PDBsum; 2OMX; -.
DR PDBsum; 2OMY; -.
DR PDBsum; 2OMZ; -.
DR AlphaFoldDB; P0DJM0; -.
DR SMR; P0DJM0; -.
DR IntAct; P0DJM0; 1.
DR STRING; 169963.lmo0433; -.
DR TCDB; 8.A.43.1.12; the neat-domain containing methaemoglobin heme sequestration (n-mhs) family.
DR PaxDb; P0DJM0; -.
DR EnsemblBacteria; CAC98512; CAC98512; CAC98512.
DR GeneID; 985151; -.
DR KEGG; lmo:lmo0433; -.
DR PATRIC; fig|169963.11.peg.446; -.
DR eggNOG; COG4886; Bacteria.
DR HOGENOM; CLU_019447_3_0_9; -.
DR OMA; FGSGVWI; -.
DR PhylomeDB; P0DJM0; -.
DR BioCyc; LMON169963:LMO0433-MON; -.
DR Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR Gene3D; 2.60.40.1220; -; 1.
DR Gene3D; 2.60.40.4270; -; 3.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR014755; Cu-Rt/internalin_Ig-like.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR024634; Internalin_N.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR025875; Leu-rich_rpt_4.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR013378; Listeria/Bacterioides_rpt.
DR InterPro; IPR042229; Listeria/Bacterioides_rpt_sf.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR012569; LRR-contain_adjacent_dom.
DR InterPro; IPR032675; LRR_dom_sf.
DR Pfam; PF09479; Flg_new; 3.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF12354; Internalin_N; 1.
DR Pfam; PF12799; LRR_4; 4.
DR Pfam; PF08191; LRR_adjacent; 1.
DR SMART; SM00369; LRR_TYP; 12.
DR SUPFAM; SSF81296; SSF81296; 1.
DR TIGRFAMs; TIGR02543; List_Bact_rpt; 3.
DR PROSITE; PS50847; GRAM_POS_ANCHORING; 1.
DR PROSITE; PS51450; LRR; 14.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall; Direct protein sequencing; Leucine-rich repeat;
KW Peptidoglycan-anchor; Reference proteome; Repeat; Secreted; Signal;
KW Virulence.
FT SIGNAL 1..35
FT /evidence="ECO:0000269|PubMed:11854224"
FT CHAIN 36..770
FT /note="Internalin A"
FT /id="PRO_0000005609"
FT PROPEP 771..800
FT /note="Removed by sortase A"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000269|PubMed:11929538, ECO:0000305|PubMed:11854224,
FT ECO:0000305|PubMed:16247833, ECO:0000305|PubMed:22837151"
FT /id="PRO_0000005610"
FT DOMAIN 36..76
FT /note="LRRNT"
FT REPEAT 77..98
FT /note="LRR 1"
FT REPEAT 99..120
FT /note="LRR 2"
FT REPEAT 121..142
FT /note="LRR 3"
FT REPEAT 143..164
FT /note="LRR 4"
FT REPEAT 165..186
FT /note="LRR 5"
FT REPEAT 187..207
FT /note="LRR 6"
FT REPEAT 208..229
FT /note="LRR 7"
FT REPEAT 230..251
FT /note="LRR 8"
FT REPEAT 252..273
FT /note="LRR 9"
FT REPEAT 274..295
FT /note="LRR 10"
FT REPEAT 296..317
FT /note="LRR 11"
FT REPEAT 318..339
FT /note="LRR 12"
FT REPEAT 340..361
FT /note="LRR 13"
FT REPEAT 362..383
FT /note="LRR 14"
FT REPEAT 384..405
FT /note="LRR 15"
FT DOMAIN 416..505
FT /note="LRRCT"
FT REPEAT 518..587
FT /note="B-1"
FT REPEAT 588..657
FT /note="B-2"
FT REPEAT 658..706
FT /note="B-3"
FT REGION 518..706
FT /note="3 X approximate tandem repeats, type B"
FT REGION 705..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 767..771
FT /note="LPXTG sorting signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:10736172"
FT MOD_RES 770
FT /note="Pentaglycyl murein peptidoglycan amidated threonine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00477,
FT ECO:0000305|PubMed:10736172"
FT VARIANT 3
FT /note="K -> R (in strain: H4)"
FT VARIANT 19
FT /note="F -> L (in strain: H4)"
FT VARIANT 51
FT /note="T -> A (in strain: EGD-SmR / Serovar 1/2a)"
FT VARIANT 94
FT /note="V -> L (in strain: EGD-SmR / Serovar 1/2a, F4233 /
FT Serotype 1/2b, F6789 / Serotype 1/2b, F5782 / Serotype 4b
FT and H4)"
FT VARIANT 118
FT /note="N -> D (in strain: EGD-SmR / Serovar 1/2a, F4233 /
FT Serotype 1/2b, F6789 / Serotype 1/2b, F5782 / Serotype 4b
FT and H4)"
FT VARIANT 142
FT /note="T -> S (in strain: F5782 / Serotype 4b and H4)"
FT VARIANT 187
FT /note="S -> N (in strain: EGD-SmR / Serovar 1/2a, F4233 /
FT Serotype 1/2b, F6789 / Serotype 1/2b and H4)"
FT VARIANT 193
FT /note="F -> L (in strain: F5782 / Serotype 4b, F4233 /
FT Serotype 1/2b and F6789 / Serotype 1/2b)"
FT VARIANT 253
FT /note="L -> W (in strain: F4233 / Serotype 1/2b and F6789 /
FT Serotype 1/2b)"
FT VARIANT 292
FT /note="S -> P (in strain: F4233 / Serotype 1/2b and F5782 /
FT Serotype 4b)"
FT VARIANT 292
FT /note="S -> R (in strain: F6789 / Serotype 1/2b)"
FT VARIANT 321
FT /note="N -> S (in strain: H4)"
FT VARIANT 381
FT /note="N -> S (in strain: H4)"
FT VARIANT 416
FT /note="A -> E (in strain: F4233 / Serotype 1/2b, F6789 /
FT Serotype 1/2b and F5782 / Serotype 4b)"
FT VARIANT 454
FT /note="T -> A (in strain: EGD-SmR / Serovar 1/2a and H4)"
FT VARIANT 474
FT /note="S -> N (in strain: H4)"
FT VARIANT 476
FT /note="P -> S (in strain: H4)"
FT VARIANT 500
FT /note="V -> A (in strain: EGD-SmR / Serovar 1/2a and H4)"
FT VARIANT 530
FT /note="H -> Y (in strain: H4)"
FT VARIANT 558
FT /note="N -> D (in strain: H4)"
FT VARIANT 573
FT /note="D -> E (in strain: EGD-SmR / Serovar 1/2a)"
FT VARIANT 594
FT /note="A -> P (in strain: EGD-SmR / Serovar 1/2a)"
FT VARIANT 648
FT /note="S -> T (in strain: H4)"
FT VARIANT 664
FT /note="A -> T (in strain: H4)"
FT VARIANT 729
FT /note="P -> S (in strain: H4)"
FT VARIANT 738
FT /note="D -> N (in strain: H4)"
FT VARIANT 781
FT /note="L -> I (in strain: H4)"
FT VARIANT 790
FT /note="M -> V (in strain: H4)"
FT MUTAGEN 150
FT /note="F->A: No longer binds human cadherin-1 (CDH1) domain
FT 1."
FT /evidence="ECO:0000269|PubMed:12526809"
FT MUTAGEN 192
FT /note="S->N: 40-fold increased affinity for human CDH1
FT domain 1. 6700-fold increased affinity for CDH1, better
FT adhesion to human Caco cells, 1000-fold more virulent in
FT mice; when associated with S-369."
FT /evidence="ECO:0000269|PubMed:17540170,
FT ECO:0000269|PubMed:17715295"
FT MUTAGEN 194
FT /note="G->SS: Increased affinity for human CDH1 domain 1."
FT /evidence="ECO:0000269|PubMed:17715295"
FT MUTAGEN 343
FT /note="Y->A: No longer binds human CDH1 domain 1."
FT /evidence="ECO:0000269|PubMed:12526809"
FT MUTAGEN 347
FT /note="Y->A: Decreased affinity for human CDH1 domain 1."
FT /evidence="ECO:0000269|PubMed:12526809"
FT MUTAGEN 367
FT /note="F->A: No longer binds human CDH1 domain 1."
FT /evidence="ECO:0000269|PubMed:12526809"
FT MUTAGEN 369
FT /note="Y->A: Increased affinity for human CDH1 domain 1."
FT /evidence="ECO:0000269|PubMed:12526809,
FT ECO:0000269|PubMed:17715295"
FT MUTAGEN 369
FT /note="Y->S: 170-fold increased affinity for human CDH1
FT domain 1. 6700-fold increased affinity for CDH1, better
FT adhesion to human Caco cells, 1000-fold more virulent in
FT mice; when associated with N-192."
FT /evidence="ECO:0000269|PubMed:17540170,
FT ECO:0000269|PubMed:17715295"
FT MUTAGEN 387
FT /note="W->A: No longer binds human CDH1 domain 1."
FT /evidence="ECO:0000269|PubMed:12526809"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 72..76
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 136..138
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 146..148
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 167..176
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 189..196
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 201..203
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 223..227
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 245..249
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 255..257
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 267..271
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 276..279
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 320..323
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 342..345
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 355..359
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1O6V"
FT HELIX 399..401
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 426..431
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 445..448
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 452..454
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 457..461
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 467..479
FT /evidence="ECO:0007829|PDB:1O6V"
FT STRAND 482..494
FT /evidence="ECO:0007829|PDB:1O6V"
SQ SEQUENCE 800 AA; 86493 MW; 4D1B03A5CF7CCDE3 CRC64;
MRKKRYVWLK SILVAILVFG SGVWINTSNG TNAQAATITQ DTPINQIFTD TALAEKMKTV
LGKTNVTDTV SQTDLDQVTT LQADRLGIKS IDGVEYLNNL TQINFSNNQL TDITPLKNLT
KLVDILMNNN QIADITPLAN LTNLTGLTLF NNQITDIDPL KNLTNLNRLE LSSNTISDIS
ALSGLTSLQQ LSFGNQVTDL KPLANLTTLE RLDISSNKVS DISVLAKLTN LESLIATNNQ
ISDITPLGIL TNLDELSLNG NQLKDIGTLA SLTNLTDLDL ANNQISNLAP LSGLTKLTEL
KLGANQISNI SPLAGLTALT NLELNENQLE DISPISNLKN LTYLTLYFNN ISDISPVSSL
TKLQRLFFYN NKVSDVSSLA NLTNINWLSA GHNQISDLTP LANLTRITQL GLNDQAWTNA
PVNYKANVSI PNTVKNVTGA LIAPATISDG GSYTEPDITW NLPSYTNEVS YTFSQPVTIG
KGTTTFSGTV TQPLKAIFNV KFHVDGKETT KEVEAGNLLT EPAKPVKEGH TFVGWFDAQT
GGTKWNFSTD KMPTNDINLY AQFSINSYTA TFDNDGVTTS QTVDYQGLLQ EPTAPTKEGY
TFKGWYDAKT GGDKWDFATS KMPAKNITLY AQYSANSYTA TFDVDGKSTT QAVDYQGLLK
EPKAPTKAGY TFKGWYDEKT DGKKWDFATD KMPANDITLY AQFTKNPVAP PTTGGNTPPT
TNNGGNTTPP SANIPGSDTS NTSTGNSAST TSTMNAYDPY NSKEASLPTT GDSDNALYLL
LGLLAVGTAM ALTKKARASK
