EATA_ECOH1
ID EATA_ECOH1 Reviewed; 1364 AA.
AC Q84GK0; E3PP92;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Serine protease EatA;
DE EC=3.4.21.-;
DE AltName: Full=Autotransporter protein EatA;
DE AltName: Full=ETEC autotransporter A;
DE Contains:
DE RecName: Full=Secreted autotransporter protein EatA;
DE Contains:
DE RecName: Full=Autotransporter protein EatA translocator;
DE Flags: Precursor;
GN Name=eatA; OrderedLocusNames=ETEC_p948_0020;
OS Escherichia coli O78:H11 (strain H10407 / ETEC).
OG Plasmid pCS1, and Plasmid p948.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316401;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF HIS-134; ASP-162 AND SER-267.
RC STRAIN=H10407 / ETEC; PLASMID=pCS1;
RX PubMed=14977988; DOI=10.1128/iai.72.3.1786-1794.2004;
RA Patel S.K., Dotson J., Allen K.P., Fleckenstein J.M.;
RT "Identification and molecular characterization of EatA, an autotransporter
RT protein of enterotoxigenic Escherichia coli.";
RL Infect. Immun. 72:1786-1794(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H10407 / ETEC; PLASMID=p948;
RX PubMed=20802035; DOI=10.1128/jb.00710-10;
RA Crossman L.C., Chaudhuri R.R., Beatson S.A., Wells T.J., Desvaux M.,
RA Cunningham A.F., Petty N.K., Mahon V., Brinkley C., Hobman J.L.,
RA Savarino S.J., Turner S.M., Pallen M.J., Penn C.W., Parkhill J.,
RA Turner A.K., Johnson T.J., Thomson N.R., Smith S.G., Henderson I.R.;
RT "A commensal gone bad: complete genome sequence of the prototypical
RT enterotoxigenic Escherichia coli strain H10407.";
RL J. Bacteriol. 192:5822-5831(2010).
CC -!- FUNCTION: Autotransporter serine protease probably involved in
CC virulence. {ECO:0000269|PubMed:14977988}.
CC -!- ACTIVITY REGULATION: Inhibited by phenylmethylsulfonyl fluoride.
CC -!- SUBCELLULAR LOCATION: [Serine protease EatA]: Periplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Secreted autotransporter protein EatA]:
CC Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Autotransporter protein EatA translocator]: Cell
CC outer membrane {ECO:0000250}; Multi-pass membrane protein
CC {ECO:0000250}. Note=The cleaved C-terminal fragment (autotransporter
CC domain) is localized in the outer membrane. {ECO:0000250}.
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, with subsequent cleavage (Probable).
CC {ECO:0000305}.
CC -!- PTM: Cleaved to release the mature protein from the outer membrane.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: Leads to accelerated virulence in the rabbit ileal loop
CC model of infection. Nevertheless, the relationship between the
CC enzymatic and potential virulence functions is uncertain.
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DR EMBL; AY163491; AAO17297.1; -; Genomic_DNA.
DR EMBL; FN649418; CBJ04449.1; -; Genomic_DNA.
DR RefSeq; WP_001045019.1; NC_017724.1.
DR AlphaFoldDB; Q84GK0; -.
DR SMR; Q84GK0; -.
DR MEROPS; N04.002; -.
DR MEROPS; S06.009; -.
DR PRIDE; Q84GK0; -.
DR EnsemblBacteria; CBJ04449; CBJ04449; ETEC_p948_0020.
DR KEGG; elh:ETEC_p948_0020; -.
DR HOGENOM; CLU_000723_0_0_6; -.
DR OMA; WVLTGYQ; -.
DR Proteomes; UP000006877; Plasmid p948.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR000710; Peptidase_S6.
DR InterPro; IPR030396; Peptidase_S6_dom.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF02395; Peptidase_S6; 1.
DR PRINTS; PR00921; IGASERPTASE.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF50494; SSF50494; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
DR PROSITE; PS51691; PEPTIDASE_S6; 1.
PE 1: Evidence at protein level;
KW Cell outer membrane; Hydrolase; Membrane; Periplasm; Plasmid; Protease;
KW Secreted; Serine protease; Signal; Transmembrane;
KW Transmembrane beta strand; Virulence; Zymogen.
FT SIGNAL 1..56
FT /evidence="ECO:0000255"
FT CHAIN 57..1364
FT /note="Serine protease EatA"
FT /id="PRO_0000026952"
FT CHAIN 57..1098
FT /note="Secreted autotransporter protein EatA"
FT /id="PRO_0000387591"
FT CHAIN 1099..1364
FT /note="Autotransporter protein EatA translocator"
FT /evidence="ECO:0000255"
FT /id="PRO_0000026953"
FT DOMAIN 57..307
FT /note="Peptidase S6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01028"
FT DOMAIN 1098..1364
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT ACT_SITE 134
FT /note="Charge relay system"
FT ACT_SITE 162
FT /note="Charge relay system"
FT ACT_SITE 267
FT /note="Charge relay system"
FT SITE 1098..1099
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT MUTAGEN 134
FT /note="H->R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14977988"
FT MUTAGEN 162
FT /note="D->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14977988"
FT MUTAGEN 267
FT /note="S->G: Loss of activity."
FT /evidence="ECO:0000269|PubMed:14977988"
SQ SEQUENCE 1364 AA; 147696 MW; 33B341FDAB6859E2 CRC64;
MNKVFSLKYS FLAKGFIAVS ELARRVSVKG KLKSASSIII SPITIAIVSY APPSLAATVN
ADISYQTFRD FAENKGAFIV GASNINIYDK NGVLVGVLDK APMPDFSSAT MNTGTLPPGD
HTLYSPQYVV TAKHVNGSDI MSFGHIQNNY TVVGENNHNS LDIKIRRLNK IVTEVAPAEI
SSVGAVNGAY QEGGRFKAFY RLGGGLQYIK DKNGNLTPVY TNGGFLTGGT ISALSSYNNG
QMITAPTGDI FNPANGPLAN YLNKGDSGSP LFAYDSLDKK WVLVGVLSSG SEHGNNWVVT
TQDFLHQQPK HDFDKTISYD SEKGSLQWRY NKNSGVGTLS QESVVWDMHG KKGGDLNAGK
NLQFTGNNGE IILHDSIDQG AGYLQFFDNY TVTSLTDQTW TGGGIITEKG VNVLWQVNGV
NDDNLHKVGE GTLTVNGKGV NNGGLKVGDG TVILNQRPDD NGHKQAFSSI NISSGRATVI
LSDANQVNPD KISWGYRGGT LDLNGNNVNF TRLQAADYGA IVSNNNKNKS ELTLKLQTLN
ENDISVDVKT YEVFGGHGSP GDLYYVPASN TYFILKSKAY GPFFSDLDNT NVWQNVGHDR
DKAIQIVKQQ KIGESSQPYM FHGQLNGYMD VNIHPLSGKD VLTLDGSVNL PEGVITKKSG
TLIFQGHPVI HAGMTTSAGQ SDWENRQFTM DKLRLDAATF HLSRNAHMQG DISAANGSTV
ILGSSRVFTD KNDGTGNAVS SVEGSSIATT AGDQSYYSGN VLLENHSSLE VRENFTGGIE
AYDSSVSVTS QNAIFDHVGS FVNSSLLLEK GAKLTAQSGI FTNNTMKIKE NASLTLTGIP
SVGKPGYYSP VTSTTEGIHL GERASLSVKN MGYLSSNITA ENSAAIINLG DSNATIGKTD
SPLFSTLMRG YNAVLQGNIM GPQSSVNMNN ALWHSDRNSE LKELKANDSQ IELGVRGHFA
KLRVKELIAS NSVFLVHANN SQADQLNVTD KLQGSNNTIL VDFFNKAANG TNVTLITAPK
GSDENTFKAG TQQIGFSNIT PEIRTENTDT ATQWVLTGYQ SVADARASKI ATDFMDSGYK
SFLTEVNNLN KRMGDLRDSQ GDAGGWARIM NGTGSGESGY RDNYTHVQIG ADRKHELNGI
DLFTGALLTY TDNNASSQAF SGKTKSLGGG VYASGLFESG AYFDLIGKYL HHDNRYTLNF
ASLGERSYTS HSLYAGAEIG YRYHMSENTW VEPQMELVYG SVSGKSFNWK DQGMQLSMKD
KDYHPLIGRT GVDVGRAFSG DTWKVTVRAG LGYQFDLLAN GETVLQDASG KKHFKGEKDS
RMLMNVGTNV EVKDNMRFGL ELEKSAFGRY NIDNSINANF RYYF
