ID B9VVY2_ECOLX Unreviewed; 948 AA.
AC B9VVY2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Intimin {ECO:0000256|ARBA:ARBA00017346};
DE AltName: Full=Attaching and effacing protein {ECO:0000256|ARBA:ARBA00029955};
GN Name=eae {ECO:0000313|EMBL:ACM67156.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACM67156.1};
RN [1] {ECO:0000313|EMBL:ACM67156.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=106G6 {ECO:0000313|EMBL:ACM67159.1}, and 41E8
RC {ECO:0000313|EMBL:ACM67156.1};
RA Lacher D.W., Steinsland H., Whittam T.S.;
RT "A revised system of nomenclature for allelic variants of intimin (eae).";
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane
CC {ECO:0000256|ARBA:ARBA00004203}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004203}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the intimin/invasin family.
CC {ECO:0000256|ARBA:ARBA00010116}.
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DR EMBL; FJ609811; ACM67156.1; -; Genomic_DNA.
DR EMBL; FJ609814; ACM67159.1; -; Genomic_DNA.
DR RefSeq; WP_032202622.1; NZ_PQQX01000059.1.
DR AlphaFoldDB; B9VVY2; -.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:InterPro.
DR Gene3D; 2.60.40.1080; -; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 2.
DR Gene3D; 2.40.160.160; Inverse autotransporter, beta-domain; 1.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR InterPro; IPR003344; Big_1_dom.
DR InterPro; IPR003343; Big_2.
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; IPR018392; LysM_dom.
DR PANTHER; PTHR39576; ATTACHING AND EFFACING PROTEIN HOMOLOG-RELATED-RELATED; 1.
DR PANTHER; PTHR39576:SF1; INVASIN-RELATED; 1.
DR Pfam; PF02369; Big_1; 2.
DR Pfam; PF02368; Big_2; 1.
DR Pfam; PF11924; IAT_beta; 1.
DR Pfam; PF07979; Intimin_C; 1.
DR Pfam; PF01476; LysM; 1.
DR PRINTS; PR01369; INTIMIN.
DR SMART; SM00634; BID_1; 2.
DR SMART; SM00635; BID_2; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 3.
DR PROSITE; PS51127; BIG1; 2.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Cell outer membrane {ECO:0000256|ARBA:ARBA00023237};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 63..112
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 560..653
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 660..755
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
SQ SEQUENCE 948 AA; 103512 MW; C1C768469D062E58 CRC64;
MITHGFYART RHKHKLKKTF IMLSAGLGLF FYVNQNSFAN GENYFKLGSD SKLLTHNSYQ
NRLFYTLKTG ETVADLSKSQ DINLSTIWSL NKHLYSSESE MMKAAPGQQI ILPLKKLPFE
YSALPLLGSA PLVAAGGVAG HTNKMTKMSP DVAKSNMTDD KALNYAAQQA ASLGSQLQSR
SLNGDYAKDT ALGIAGNQAS SQLQAWLQHY GTAEVNLQSG NNFDGSSLDF LLPFYDSEKM
LAFGQVGARY IDSRFTANLG AGQRFFLPEN MLGYNVFIDQ DFSGDNTRLG IGGEYWRDYF
KSSVNGYFRM SGWHESYNKK DYDERPANGF DIRFNGYLPS YPALGAKLMY EQYYGDNVAL
FNSDKLQSNP GAATVGVNYT PIPLVTMGID YRHGTGNEND LLYSMQFRYQ FDKPWSQQIE
PQYVNELRTL SGSRYDLVQR NNNIILEYKK QDILSLNIPH DINGTERSTQ KIQLIVKSKY
GLDRIVWDDS SLRSQGGQIQ HSGSQSAQDY QAILPAYVQG GSNVYKVTAR AYDRNGNSSN
NVQLTITVLS NGQVVDQVGV TDFTADKTSA KADNADTITY TATVKKNGVA QANAPVTFSI
VSGTATLGAN SAKTDSNGKA TVTLKSSTPG QVVVSAKTAE MTSALNASAV IFVEQTKASI
TEIKADKTTA KANGSDAITY TVKVMKNNQP EANHSVTFST NFGKLDGNSN TQTVKTDENG
KATVKLTSGA EGSAVVSAKV SEINTEVKAP EVKFFSVLSI DNNVNIIGTS ANAALPNIWL
QYGQFKLTAK GGDGKYKWHS KDTSVASVDA STGQVTLLKK GTTTIEVVSG DNQTAAYTIN
TPDKIISVES QNTEIYSSAE KTCSINSGRL PLSTNELKDV YSKWGAANSY ERYKDKNTIA
AWTQQTEEDK KAGWTSTFDI VTQNEIPSNG SNSKVDVKKA NGFAVCVR
//
