ESIB_ECOL6
ID ESIB_ECOL6 Reviewed; 490 AA.
AC A0A0H2VDN9;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 27.
DE RecName: Full=Secretory immunoglobulin A-binding protein EsiB {ECO:0000303|PubMed:23882011};
DE Flags: Precursor;
GN Name=esiB {ECO:0000303|PubMed:23882011}; OrderedLocusNames=c5321;
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 PROTEIN SEQUENCE OF 244-260, FUNCTION IN INFECTION, INTERACTION WITH HUMAN
RP SECRETED IGA, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=23882011; DOI=10.1128/mbio.00206-13;
RA Pastorello I., Rossi Paccani S., Rosini R., Mattera R., Ferrer Navarro M.,
RA Urosev D., Nesta B., Lo Surdo P., Del Vecchio M., Rippa V., Bertoldi I.,
RA Gomes Moriel D., Laarman A.J., van Strijp J.A., Daura X., Pizza M.,
RA Serino L., Soriani M.;
RT "EsiB, a novel pathogenic Escherichia coli secretory immunoglobulin A-
RT binding protein impairing neutrophil activation.";
RL MBio 4:E00206-E00206(2013).
RN [3]
RP IDENTIFICATION, AND BIOTECHNOLOGY.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=20439758; DOI=10.1073/pnas.0915077107;
RA Moriel D.G., Bertoldi I., Spagnuolo A., Marchi S., Rosini R., Nesta B.,
RA Pastorello I., Corea V.A., Torricelli G., Cartocci E., Savino S.,
RA Scarselli M., Dobrindt U., Hacker J., Tettelin H., Tallon L.J.,
RA Sullivan S., Wieler L.H., Ewers C., Pickard D., Dougan G., Fontana M.R.,
RA Rappuoli R., Pizza M., Serino L.;
RT "Identification of protective and broadly conserved vaccine antigens from
RT the genome of extraintestinal pathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:9072-9077(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 24-490 IN COMPLEX WITH MAGNESIUM,
RP AND COFACTOR.
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=24099525; DOI=10.1186/1472-6807-13-19;
RA Urosev D., Ferrer-Navarro M., Pastorello I., Cartocci E., Costenaro L.,
RA Zhulenkovs D., Marechal J.D., Leonchiks A., Reverter D., Serino L.,
RA Soriani M., Daura X.;
RT "Crystal structure of c5321: a protective antigen present in uropathogenic
RT Escherichia coli strains displaying an SLR fold.";
RL BMC Struct. Biol. 13:19-19(2013).
CC -!- FUNCTION: Upon host (human neutrophil) infection interferes with
CC productive FCAR signaling, inhibiting secreted IgA (SIgA) effector
CC functions and probably avoiding neutrophil activation. Inhibits the
CC SIgA-mediated oxidative burst by neutrophils, decreases generation of
CC ROS (reactive oxygen species) by neutrophils and reduces chemotaxis by
CC neutrophils, all of which are SIgA effector functions used to stimulate
CC the immune response. Does not block SIgA-binding to its receptor (FCAR)
CC on neutrophils, but it decreases SIgA-stimulated phosphorylation of
CC cytoplasmic proteins, including phospholipase C-gamma and MAP kinases,
CC all actions that may be advantageous to the pathogen.
CC {ECO:0000269|PubMed:23882011}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:24099525};
CC Note=The physiological metal is unknown. {ECO:0000305|PubMed:24099525};
CC -!- SUBUNIT: Interacts with human secreted IgA (SIgA) at least via resides
CC 244-260. {ECO:0000269|PubMed:23882011}.
CC -!- SUBCELLULAR LOCATION: Cell surface {ECO:0000269|PubMed:23882011}.
CC Note=Accumulates at 1 cell pole in the bladder of mice infected with
CC this strain, in overexpressing bacteria the protein is found all over
CC the cell surface but not in the secreted fraction (PubMed:23882011).
CC Human blood sera from clinical patients with urinary tract infections
CC reacts with antibodies to this protein (PubMed:23882011).
CC {ECO:0000269|PubMed:23882011}.
CC -!- INDUCTION: More highly transcribed in logarithmic than stationary
CC phase. Protein is not detected in bacteria growing in culture but is
CC detected upon infection of mice (at protein level).
CC {ECO:0000269|PubMed:23882011}.
CC -!- BIOTECHNOLOGY: Immunizes 1/3 of injected mice against subsequent
CC infection with E.coli strain CFT073, suggesting it might be a good
CC vaccine candidate for ExPEC (extraintestinal pathogenic E.coli)
CC strains. {ECO:0000269|PubMed:20439758}.
CC -!- MISCELLANEOUS: Preferentially encoded in ExPEC strains (extraintestinal
CC pathogenic E.coli). {ECO:0000305|PubMed:23882011}.
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DR EMBL; AE014075; AAN83742.1; -; Genomic_DNA.
DR RefSeq; WP_000749215.1; NC_004431.1.
DR PDB; 4BWR; X-ray; 1.74 A; A=24-490.
DR PDBsum; 4BWR; -.
DR AlphaFoldDB; A0A0H2VDN9; -.
DR SMR; A0A0H2VDN9; -.
DR STRING; 199310.c5321; -.
DR EnsemblBacteria; AAN83742; AAN83742; c5321.
DR KEGG; ecc:c5321; -.
DR eggNOG; COG0790; Bacteria.
DR HOGENOM; CLU_000288_36_14_6; -.
DR OMA; CEEWYER; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0019862; F:IgA binding; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050777; P:negative regulation of immune response; IDA:UniProtKB.
DR GO; GO:1902564; P:negative regulation of neutrophil activation; IDA:UniProtKB.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006597; Sel1-like.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR Pfam; PF08238; Sel1; 11.
DR SMART; SM00671; SEL1; 11.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Magnesium; Metal-binding; Repeat;
KW Signal; Virulence.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..490
FT /note="Secretory immunoglobulin A-binding protein EsiB"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434574"
FT REPEAT 39..74
FT /note="Sel1-like 1"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 77..109
FT /note="Sel1-like 2"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 111..145
FT /note="Sel1-like 3"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 153..182
FT /note="Sel1-like 4"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 185..218
FT /note="Sel1-like 5"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 222..254
FT /note="Sel1-like 6"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 256..290
FT /note="Sel1-like 7"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 291..327
FT /note="Sel1-like 8"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 328..361
FT /note="Sel1-like 9"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 364..397
FT /note="Sel1-like 10"
FT /evidence="ECO:0000303|PubMed:24099525"
FT REPEAT 399..430
FT /note="Sel1-like 11"
FT /evidence="ECO:0000303|PubMed:24099525"
FT BINDING 122
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24099525"
FT BINDING 159
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24099525"
FT BINDING 161
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:24099525"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 39..51
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 59..71
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 75..87
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 95..107
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 111..123
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 131..143
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 147..159
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 167..179
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 183..195
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 203..215
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 219..231
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 239..250
FT /evidence="ECO:0007829|PDB:4BWR"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 255..267
FT /evidence="ECO:0007829|PDB:4BWR"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 275..287
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 291..303
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 312..324
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 328..340
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 344..359
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 363..375
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 377..379
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 383..395
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 399..411
FT /evidence="ECO:0007829|PDB:4BWR"
FT STRAND 413..415
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 419..433
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 436..446
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 451..468
FT /evidence="ECO:0007829|PDB:4BWR"
FT HELIX 470..479
FT /evidence="ECO:0007829|PDB:4BWR"
SQ SEQUENCE 490 AA; 54835 MW; 64ADB86117832A99 CRC64;
MKKSLLAVML TGLFALVSLP ALGNVNLEQL KQKAESGEAK AQLELGYRYF QGNETTKDLT
QAMDWFRRAA EQGYTPAEYV LGLRYMNGEG VPQDYAQAVI WYKKAALKGL PQAQQNLGVM
YHEGNGVKVD KAESVKWFRL AAEQGRDSGQ QSMGDAYFEG DGVTRDYVMA REWYSKAAEQ
GNVWSCNQLG YMYSRGLGVE RNDAISAQWY RKSATSGDEL GQLHLADMYY FGIGVTQDYT
QSRVLFSQSA EQGNSIAQFR LGYILEQGLA GAKEPLKALE WYRKSAEQGN SDGQYYLAHL
YDKGAEGVAK NREQAISWYT KSAEQGDATA QANLGAIYFR LGSEEEHKKA VEWFRKAAAK
GEKAAQFNLG NALLQGKGVK KDEQQAAIWM RKAAEQGLSA AQVQLGEIYY YGLGVERDYV
QAWAWFDTAS TNDMNLFGTE NRNITEKKLT AKQLQQAELL SQQYIEKYAP EAWARMQKLK
AQSAVKTGNK
