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
//