EHAG_ECO57
ID EHAG_ECO57 Reviewed; 1588 AA.
AC Q7DJ60; Q8XDG4;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Autotransporter adhesin EhaG {ECO:0000305};
DE AltName: Full=Type 5 secretion system autotransporter EhaG {ECO:0000305};
DE Flags: Precursor;
GN Name=ehaG {ECO:0000303|PubMed:22286983};
GN Synonyms=H161 {ECO:0000312|EMBL:BAB87814.1};
GN OrderedLocusNames=ECs4480 {ECO:0000312|EMBL:BAB37903.1},
GN Z5029 {ECO:0000312|EMBL:AAG58749.1};
GN ORFNames=A8V30_24325 {ECO:0000312|EMBL:ANG82226.1},
GN A8V31_24315 {ECO:0000312|EMBL:ANG71048.1},
GN A8V32_24030 {ECO:0000312|EMBL:ANG76544.1},
GN JEONG1266_25035 {ECO:0000312|EMBL:AMG81107.1};
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RA Makino K., Yutsudo C.H., Yokoyama K., Kubota Y., Kimura S., Shinagawa H.;
RT "O157 specific gene similar to H. influenzae adhesin gene.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / JEONG-1266 / STEC;
RX PubMed=27056233; DOI=10.1128/genomea.00258-16;
RA Teng L., Ginn A., Jeon S., Kang M., Jeong K.C.;
RT "Complete genome sequence of an Escherichia coli O157:H7 strain isolated
RT from a super-shedder steer.";
RL Genome Announc. 4:E00258-E00258(2016).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FRIK2069, FRIK2455, and FRIK2533;
RA Kasper C., Jeong K.C., Ginn A.;
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, AND INDUCTION.
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=22286983; DOI=10.1128/aem.06680-11;
RA Totsika M., Wells T.J., Beloin C., Valle J., Allsopp L.P., King N.P.,
RA Ghigo J.M., Schembri M.A.;
RT "Molecular characterization of the EhaG and UpaG trimeric autotransporter
RT proteins from pathogenic Escherichia coli.";
RL Appl. Environ. Microbiol. 78:2179-2189(2012).
CC -!- FUNCTION: Mediates aggregation, biofilm formation and adhesion to a
CC range of extracellular matrix (ECM) proteins, such as fibronectin,
CC fibrinogen, laminin and collagen types I, II, III, and V. Mediates
CC adhesion to intestinal epithelial cells. {ECO:0000269|PubMed:22286983}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:A0A0H2VCA1}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000250|UniProtKB:A0A0H2VCA1}.
CC Cell outer membrane {ECO:0000250|UniProtKB:A0A0H2VCA1}. Note=The C-
CC terminal translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface.
CC {ECO:0000250|UniProtKB:A0A0H2VCA1}.
CC -!- INDUCTION: Expression is negatively regulated by H-NS.
CC {ECO:0000269|PubMed:22286983}.
CC -!- DOMAIN: The signal peptide, cleaved at the inner membrane, guides the
CC autotransporter protein to the periplasmic space. Then, insertion of
CC the C-terminal translocator domain in the outer membrane forms a
CC hydrophilic pore for the translocation of the passenger domain to the
CC bacterial cell surface. {ECO:0000250|UniProtKB:A0A0H2VCA1}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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DR EMBL; AB036416; BAB87814.1; -; Genomic_DNA.
DR EMBL; AE005174; AAG58749.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37903.1; -; Genomic_DNA.
DR EMBL; CP014314; AMG81107.1; -; Genomic_DNA.
DR EMBL; CP015842; ANG71048.1; -; Genomic_DNA.
DR EMBL; CP015843; ANG76544.1; -; Genomic_DNA.
DR EMBL; CP015846; ANG82226.1; -; Genomic_DNA.
DR PIR; A86036; A86036.
DR PIR; H91188; H91188.
DR RefSeq; NP_312507.1; NC_002695.1.
DR RefSeq; WP_001033191.1; NZ_SEKU01000021.1.
DR AlphaFoldDB; Q7DJ60; -.
DR SMR; Q7DJ60; -.
DR STRING; 155864.EDL933_4866; -.
DR EnsemblBacteria; AAG58749; AAG58749; Z5029.
DR EnsemblBacteria; BAB37903; BAB37903; ECs_4480.
DR GeneID; 915578; -.
DR KEGG; ece:Z5029; -.
DR KEGG; ecs:ECs_4480; -.
DR PATRIC; fig|386585.9.peg.4695; -.
DR eggNOG; COG5295; Bacteria.
DR HOGENOM; CLU_002363_1_0_6; -.
DR OMA; VYTTGSE; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; -; 4.
DR InterPro; IPR008640; Adhesin_Head_dom.
DR InterPro; IPR008635; Coiled_stalk_dom.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR045584; Pilin-like.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR InterPro; IPR005594; YadA_C.
DR Pfam; PF13018; ESPR; 1.
DR Pfam; PF03895; YadA_anchor; 1.
DR Pfam; PF05658; YadA_head; 9.
DR Pfam; PF05662; YadA_stalk; 12.
DR SUPFAM; SSF101967; SSF101967; 9.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 2: Evidence at transcript level;
KW Cell outer membrane; Membrane; Protein transport; Reference proteome;
KW Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..53
FT /evidence="ECO:0000255"
FT CHAIN 54..1588
FT /note="Autotransporter adhesin EhaG"
FT /id="PRO_0000437738"
FT TRANSMEM 1534..1544
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1548..1558
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1567..1573
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1577..1588
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 54..1499
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000305"
FT REGION 1500..1588
FT /note="Translocator domain"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1588 AA; 160151 MW; B2BA4E06EFF28DEC CRC64;
MNKIFKVIWN PATGNYTVTS ETAKSRGKKS GRSKLLISAL VAGGMLSSFG ALANAGNDNG
QGVDYGSGSA GDGWVAIGKG AKANTFMNTS GSSTAVGYDA IAEGQYSSAI GSKTHAIGGA
SMAFGVSAIS EGDRSIALGA SSYSLGQYSM ALGRYSKALG KLSIAMGDSS KAEGANAIAL
GNATKATEIM SIALGDTANA SKAYSMALGA SSVASEENAI AIGAETEAAE NATAIGNNAK
AKGTNSMAMG FGSLADKVNT IALGNGSQAL ADNAIAIGQG NKADGVDAIA LGNGSQSRGL
NTIALGTASN ATGDKSLALG SNSSANGINS VALGADSIAD LDNTVSVGNS SLKRKIVNVK
NGAIKSDSYD AINGSQLYAI SDSVAKRLGG GAAVDVDDGT VTAPTYNLKN GSKNNVGAAL
AVLDENTLQW DQTKGKYSAA HGTSSPTASV ITDVADGTIS ASSKDAVNGS QLKATNDDVE
ANTANIATNT SNIATNTANI ATNTTNITNL TDSVGDLQAD ALLWNETKKA FSAAHGQDTT
SKITNVKDAD LTADSTDAVN GSQLKTTNDA VATNTTNIAN NTSNIATNTT NISNLTETVT
NLGEDALKWD KDNGVFTAAH GTETTSKITN VKDGDLTTGS TDAVNGSQLK TTNDAVATNT
TNIATNTTNI SNLTETVTNL GEDALKWDKD NGVFTAAHGN NTASKITNIL DGTVTATSSD
AINGSQLYDL SSNIATYFGG NASVNTDGVF TGPTYKIGET NYYNVGDALA AINSSFSTSL
GDALLWDATA GKFSAKHGTN GDASVITDVA DGEISDSSSD AVNGSQLHGV SSYVVDALGG
GAEVNADGTI TAPTYTIANA DYDNVGDALN AIDTTLDDAL LWDADAGENG AFSAAHGKDK
TASVITNVAN GAISAASSDA INGSQLYTTN KYIADALGGD AEVNADGTIT APTYTIANAE
YNNVGDALDA LDDNALLWDE TANGGAGAYN ASHDGKASII TNVANGSISE DSTDAVNGSQ
LNATNMMIEQ NTQIINQLAG NTDATYIQEN GAGINYVRTN DDGLAFNDAS AQGVGATAIG
YNSVAKGDSS VAIGQGSYSD VDTGIALGSS SVSSRVIAKG SRDTSITENG VVIGYDTTDG
ELLGALSIGD DGKYRQIINV ADGSEAHDAV TVRQLQNAIG AVATTPTKYF HANSTEEDSL
AVGTDSLAMG AKTIVNGDKG IGIGYGAYVD ANALNGIAIG SNAQVIHVNS IAIGNGSTTT
RGAQTNYTAY NMDAPQNSVG EFSVGSADGQ RQITNVAAGS ADTDAVNVGQ LKVTDAQVSQ
NTQSITNLDN RVTNLDSRVT NIENGIGDIV TTGSTKYFKT NTDGVDASAQ GKDSVAIGSG
SIAAADNSVA LGTGSVATEE NTISVGSSTN QRRITNVAAG KNATDAVNVA QLKSSEAGGV
RYDTKADGSI DYSNITLGGG NGGTTRISNV SAGVNNNDVV NYAQLKQSVQ ETKQYTDQRM
VEMDNKLSKT ESKLSGGIAS AMAMTGLPQA YTPGASMASI GGGTYNGESA VALGVSMVSA
NGRWVYKLQG STNSQGEYSA ALGAGIQW
