UPAG_ECOL6
ID UPAG_ECOL6 Reviewed; 1778 AA.
AC A0A0H2VCA1;
DT 02-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 25-MAY-2022, entry version 31.
DE RecName: Full=Autotransporter adhesin UpaG {ECO:0000305};
DE AltName: Full=Type 5 secretion system autotransporter YadA {ECO:0000305};
DE Flags: Precursor;
GN Name=upaG {ECO:0000303|PubMed:18424525};
GN OrderedLocusNames=c4424 {ECO:0000312|EMBL:AAN82860.1};
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN [2]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=18424525; DOI=10.1128/jb.00122-08;
RA Valle J., Mabbett A.N., Ulett G.C., Toledo-Arana A., Wecker K., Totsika M.,
RA Schembri M.A., Ghigo J.M., Beloin C.;
RT "UpaG, a new member of the trimeric autotransporter family of adhesins in
RT uropathogenic Escherichia coli.";
RL J. Bacteriol. 190:4147-4161(2008).
RN [3]
RP FUNCTION, AND INDUCTION.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
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 human T24 bladder epithelial cells.
CC {ECO:0000269|PubMed:18424525, ECO:0000269|PubMed:22286983}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:18424525}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:18424525}. Cell
CC outer membrane {ECO:0000269|PubMed:18424525}. Note=The C-terminal
CC translocator domain is localized in the outer membrane and the
CC passenger domain is at the cell surface. {ECO:0000269|PubMed:18424525}.
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:0000269|PubMed:18424525}.
CC -!- SIMILARITY: Belongs to the autotransporter-2 (AT-2) (TC 1.B.40) family.
CC {ECO:0000305}.
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DR EMBL; AE014075; AAN82860.1; -; Genomic_DNA.
DR RefSeq; WP_001033292.1; NC_004431.1.
DR AlphaFoldDB; A0A0H2VCA1; -.
DR SMR; A0A0H2VCA1; -.
DR STRING; 199310.c4424; -.
DR EnsemblBacteria; AAN82860; AAN82860; c4424.
DR KEGG; ecc:c4424; -.
DR eggNOG; COG5295; Bacteria.
DR HOGENOM; CLU_002363_1_0_6; -.
DR OMA; VYTTGSE; -.
DR Proteomes; UP000001410; 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; -; 5.
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; 10.
DR Pfam; PF05662; YadA_stalk; 15.
DR SUPFAM; SSF101967; SSF101967; 11.
DR SUPFAM; SSF54523; SSF54523; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Membrane; Protein transport; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..53
FT /evidence="ECO:0000255"
FT CHAIN 54..1778
FT /note="Autotransporter adhesin UpaG"
FT /id="PRO_0000437740"
FT TRANSMEM 1724..1734
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1738..1748
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1757..1763
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT TRANSMEM 1767..1778
FT /note="Beta stranded"
FT /evidence="ECO:0000250|UniProtKB:A1JUB7"
FT REGION 54..1689
FT /note="Surface exposed passenger domain"
FT /evidence="ECO:0000305|PubMed:18424525"
FT REGION 1690..1778
FT /note="Translocator domain"
FT /evidence="ECO:0000305|PubMed:18424525"
SQ SEQUENCE 1778 AA; 177679 MW; 98564AA3A797DA20 CRC64;
MNKIFKVIWN PATGSYTVAS ETAKSRGKKS GRSKLLISAL VAGGLLSSFG ASADNYTGQP
TDYGDGSAGD GWVAIGKGAK ANTFMNTSGA STALGYDAIA EGEYSSAIGS KTLATGGASM
AFGVSAKAMG DRSVALGASS VANGDRSMAF GRYAKTNGFT SLAIGDSSLA DGEKTIALGN
TAKAYEIMSI ALGDNANASK EYAMALGASS KAGGADSLAF GRKSTANSTG SLAIGADSSS
SNDNAIAIGN KTQALGVNSM ALGNASQASG ESSIALGNTS EASEQNAIAL GQGSIASKVN
SIALGSNSLS SGENAIALGE GSAAGGSNSL AFGSQSRANG NDSVAIGVGA AAATDNSVAI
GAGSTTDASN TVSVGNSATK RKIVNMAAGA ISNTSTDAIN GSQLYTISDS VAKRLGGGAT
VGSDGTVTAV SYALRSGTYN NVGDALSGID NNTLQWNKTA GAFSANHGAN ATNKITNVAK
GTVSATSTDV VNGSQLYDLQ QDALLWNGTA FSAAHGTEAT SKITNVTAGN LTAGSTDAVN
GSQLKTTNDN VTTNTTNIAT NTTNITNLTD AVNGLGDDSL LWNKAAGAFS AAHGTEATSK
ITNVTAGNLT AGSTDAVNGS QLKTTNDNVT TNTTNIATNT TNITNLTDAV NGLGDDSLLW
NKTAGAFSAA HGTDATSKIT NVTAGNLTAG STDAVNGSQL KTTNDNVTTN TTNIATNTTN
ITNLTDAVNG LGDDSLLWNK TAGAFSAAHG TDATSKITNV KAGDLTAGST DAVNGSQLKT
TNDNVSTNTT NITNLTDAVN GLGDDSLLWN KTAGAFSAAH GTDATSKITN VKAGDLTAGS
TDAVNGSQLK TTNDNVSTNT TNITNLTDSV GDLKDDSLLW NKAAGAFSAA HGTEATSKIT
NLLAGKISSN STDAINGSQL YGVADSFTSY LGGGADISDT GVLSGPTYTI GGTDYTNVGD
ALAAINTSFS TSLGDALLWD ATAGKFSAKH GINNAPSVIT DVANGAVSST SSDAINGSQL
YGVSDYIADA LGGNAVVNTD GSITTPTYAI AGGSYNNVGD ALEAIDTTLD DALLWDTTAN
GGNGAFSAAH GKDKTASVIT NVANGAVSAT SNDAINGSQL YSTNKYIADA LGGDAEVNAD
GTITAPTYTI ANTDYNNVGE ALDALDNNAL LWDEDAGAYN ASHDGNASKI TNVAAGDLST
TSTDAVNGSQ LNATNILVTQ NSQMINQLAG NTSETYIEEN GAGINYVRTN DSGLAFNDAS
ASGIGATAVG YNAVASHASS VAIGQDSISE VDTGIALGSS SVSSRVIVKG TRNTSVSEEG
VVIGYDTTDG ELLGALSIGD DGKYRQIINV ADGSEAHDAV TVRQLQNAIG AVATTPTKYY
HANSTAEDSL AVGEDSLAMG AKTIVNGNAG IGIGLNTLVL ADAINGIAIG SNARANHADS
IAMGNGSQTT RGAQTNYTAY NMDAPQNSVG EFSVGSEDGQ RQITNVAAGS ADTDAVNVGQ
LKVTDAQVSQ NTQSITNLNT QVTNLDTRVT NIENGIGDIV TTGSTKYFKT NTDGADANAQ
GKDSVAIGSG SIAAADNSVA LGTGSVADEE NTISVGSSTN QRRITNVAAG VNATDAVNVS
QLKSSEAGGV RYDTKADGSI DYSNITLGGG NSGTTRISNV SAGVNNNDAV NYAQLKQSVQ
ETKQYTDQRM VEMDNKLSKT ESKLSGGIAS AMAMTGLPQA YTPGASMASI GGGTYNGESA
VALGVSMVSA NGRWVYKLQG STNSQGEYSA ALGAGIQW
