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Database: UniProt
Entry: B5ARW2_ECOLX
LinkDB: B5ARW2_ECOLX
Original site: B5ARW2_ECOLX 
ID   B5ARW2_ECOLX            Unreviewed;       934 AA.
AC   B5ARW2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Intimin {ECO:0000256|ARBA:ARBA00017346};
DE   AltName: Full=Attaching and effacing protein {ECO:0000256|ARBA:ARBA00029955};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ACG59735.1};
RN   [1] {ECO:0000313|EMBL:ACG59735.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=33264 {ECO:0000313|EMBL:ACG59735.1};
RA   Zhang Y., Golds G., John S.J., Laing C., Kropinski A., Gannon V.P.J.;
RL   Submitted (JUL-2008) 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; EU871628; ACG59735.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5ARW2; -.
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:SF2; ATTACHING AND EFFACING PROTEIN HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR39576; ATTACHING AND EFFACING PROTEIN HOMOLOG-RELATED-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..753
FT                   /note="Big-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51127"
SQ   SEQUENCE   934 AA;  101806 MW;  E9B338F252770002 CRC64;
     MITHGCYTRT RHKHKLKKTL IMLSAGLGLF FYVNQNSFAN GENYFKLGSD SKLLTHDSYQ
     NRLFYTLKTG ETVADLSKSQ DINLSTIWSL NKHLYSSESE MMKAAPGQQI ILPLKKLPFE
     YSALPLLGSA PLVAAGGVAG HTNKLTKMSP DVTKSNMTDD KALNYAAQQA TSLGSQLQSR
     SLNGDYAKDT ALGIAGNQAS SQLQAWLQHY GTAEVNLQSG NNFDGSSLDF LLPFYDSEKM
     LAFGQVGARY IDSRFTANLG AGQRFFLPAN MLGYNVFIDQ DFSGDNTRLG IGGEYWRDYF
     KSSVNGYFRM SGWHESYNKK DYDERPANGF DIRFNGYLPS YPALGAKLIY EQYYGDNVAL
     FNSDKLQSNP GAATVGVNYT PIPLVTMGID YHHGTGNEND LLYSMQFRYQ FDKSWSQQIE
     PQYVNELRTL SGSRYDLVQR NNNIILEYRK QDILSLNIPH DINGTEHSTQ KIQLIVKSKY
     GLDRIVWDDS ALRSQGGQIQ HSGSQSAQDY QAILPAYVQG GSNIYKVTAR AYDRNGNSSN
     NVQLTITVLS NGQVVDQVGV TDFTADKTSA KADNADTITY TATVKKNGVA QANVPVSFNI
     VSGTATLGAN SAKTDANGKA TVTLKSSTPG QVVVSAKTAE MTSALNASAV IFFDQTKASI
     TEIKADKTTA VANGKDAIKY TVKVMKNGQP VNNQSVTFST NFGMFNGKSQ TQATTGNDGR
     ATITLTSSST GKATVSAAVS DGAEVKATEV TFFDELKIDN KVDIIGNNVR GELPNIWLQY
     GQFKLKASGG DGTYSWYSEN TSIATVDASG KVTLNGKGSV VIKATSGDKQ TVSYTIKAPS
     YMIKVDKQAY YADAMSICKN LLPSTQTVLS DIYDSWGAAN KYSHYSSMNS ITAWIKQTSS
     EQSSGVSSTY NLITQNPLPG VNVNTPNVYA VCVE
//
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