ID U5Y6W4_9BACT Unreviewed; 558 AA.
AC U5Y6W4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Intimin {ECO:0000256|ARBA:ARBA00017346};
DE AltName: Full=Attaching and effacing protein {ECO:0000256|ARBA:ARBA00029955};
DE Flags: Fragment;
GN Name=eae {ECO:0000313|EMBL:AGZ84298.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AGZ84298.1};
RN [1] {ECO:0000313|EMBL:AGZ84298.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=24141131; DOI=10.1128/AEM.02747-13;
RA Yang K., Pagaling E., Yan T.;
RT "Estimating the Prevalence of Potential Enteropathogenic Escherichia coli
RT and Intimin Gene Diversity in a Human Community by Monitoring Sanitary
RT Sewage.";
RL Appl. Environ. Microbiol. 80:119-127(2014).
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; KF771369; AGZ84298.1; -; Genomic_DNA.
DR AlphaFoldDB; U5Y6W4; -.
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 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; PF11924; IAT_beta; 1.
DR Pfam; PF07979; Intimin_C; 1.
DR PRINTS; PR01369; INTIMIN.
DR SMART; SM00634; BID_1; 2.
DR SMART; SM00635; BID_2; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF49373; Invasin/intimin cell-adhesion fragments; 3.
DR PROSITE; PS51127; BIG1; 2.
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 181..274
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT DOMAIN 281..372
FT /note="Big-1"
FT /evidence="ECO:0000259|PROSITE:PS51127"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:AGZ84298.1"
SQ SEQUENCE 558 AA; 59933 MW; 4AEDBB035178BDED CRC64;
TPIPLVTMGI DYRHGTGNEN DLLYSMQFRY QFDKPWSQQI EPQYVNELRT LSGSRYDLVQ
RNNNIILEYK KQDILSLNIP HDINGTERST QKIQLIVKSK YGLDRIVWDD SSLRSQGGQI
QHSGSQSAQD YQAILPAYVQ GGSNVYKVTA RAYDRNGNSS NNVQLTITVL SNGQVVDQVG
VTDFTADKTS AKADGTEAIT YTATVKKNGV AQANVPVSFN IVSGTATLGA NSAKTDANGK
ATVTLKSSTP GQVVVSAKTA EMTSALNASA VIFVDQTKAS ITEIKADKTT AVANGKDAVT
YTVKVMKNGL PEKGHVVTFS TDLGKLNLQT VATDKDGFAS VTLTSDSVGK AVVSAKVSEA
GSVVNADAVN FFATLSIDNN VEIVGTKVRG ELPNIWLRYG QVKLNANGGN GGYSWSSDNP
DIASIDANTG IITLNKKGTT VIKVISGDKQ IATYTIKTPQ EIVSLDNSVK VKYDEASGIC
SNNAAYLSVS VDSLKKLYSQ WGPANKYSHY TQGTINAWIQ QTEQDKKDSV ATTYDIVTDN
TVINVDSTVA NAYAVCIK
//
