TIBA_ECOH1
ID TIBA_ECOH1 Reviewed; 989 AA.
AC Q9XD84; E3PBM3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Adhesin/invasin TibA autotransporter;
DE Contains:
DE RecName: Full=Adhesin/invasin TibA;
DE AltName: Full=Glycoprotein TibA;
DE Contains:
DE RecName: Full=Adhesin/invasin TibA translocator;
DE Flags: Precursor;
GN Name=tibA; OrderedLocusNames=ETEC_2141;
OS Escherichia coli O78:H11 (strain H10407 / ETEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=316401;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], GLYCOSYLATION, AND PROTEIN SEQUENCE OF
RP 55-69.
RC STRAIN=H10407 / ETEC;
RX PubMed=10417177; DOI=10.1128/iai.67.8.4084-4091.1999;
RA Lindenthal C., Elsinghorst E.A.;
RT "Identification of a glycoprotein produced by enterotoxigenic Escherichia
RT coli.";
RL Infect. Immun. 67:4084-4091(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H10407 / ETEC;
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).
RN [3]
RP ROLE IN INVASION, AND SUBCELLULAR LOCATION.
RC STRAIN=H10407 / ETEC;
RX PubMed=8039917; DOI=10.1128/iai.62.8.3463-3471.1994;
RA Elsinghorst E.A., Weitz J.A.;
RT "Epithelial cell invasion and adherence directed by the enterotoxigenic
RT Escherichia coli tib locus is associated with a 104-kilodalton outer
RT membrane protein.";
RL Infect. Immun. 62:3463-3471(1994).
RN [4]
RP ROLE IN ADHERENCE AND INVASION, AND PROTEIN SEQUENCE OF 55-64.
RC STRAIN=H10407 / ETEC;
RX PubMed=11119488; DOI=10.1128/iai.69.1.52-57.2001;
RA Lindenthal C., Elsinghorst E.A.;
RT "Enterotoxigenic Escherichia coli TibA glycoprotein adheres to human
RT intestine epithelial cells.";
RL Infect. Immun. 69:52-57(2001).
RN [5]
RP AUTOAGGREGATION, BIOFILM FORMATION, AND GLYCOSYLATION BY TIBC.
RC STRAIN=H10407 / ETEC;
RX PubMed=15784535; DOI=10.1128/iai.73.4.1954-1963.2005;
RA Sherlock O., Vejborg R.M., Klemm P.;
RT "The TibA adhesin/invasin from enterotoxigenic Escherichia coli is self
RT recognizing and induces bacterial aggregation and biofilm formation.";
RL Infect. Immun. 73:1954-1963(2005).
CC -!- FUNCTION: Mediates both adhesion to and invasion of human intestine
CC epithelial cells. Also mediates bacterial cell aggregation via
CC intercellular TibA-TibA interaction. Enhances biofilm formation.
CC {ECO:0000269|PubMed:11119488, ECO:0000269|PubMed:8039917}.
CC -!- SUBCELLULAR LOCATION: [Adhesin/invasin TibA autotransporter]: Periplasm
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Adhesin/invasin TibA]: Secreted. Cell surface.
CC -!- SUBCELLULAR LOCATION: [Adhesin/invasin TibA translocator]: Cell outer
CC membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
CC Note=The cleaved C-terminal fragment (autotransporter domain) is
CC 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 (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Glycosylated by TibC. Glycosylation is required for TibA-mediated
CC adhesion and invasion of human cells but not for aggregation.
CC {ECO:0000269|PubMed:10417177, ECO:0000269|PubMed:15784535}.
CC -!- MISCELLANEOUS: TibA-mediated aggregation is blocked upon capsule
CC expression and fimbriation and is sensitive to pH extremes.
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DR EMBL; AF109215; AAD41751.1; -; Genomic_DNA.
DR EMBL; FN649414; CBJ01643.1; -; Genomic_DNA.
DR RefSeq; WP_001045641.1; NC_017633.1.
DR PDB; 4Q1Q; X-ray; 2.11 A; A/B=55-350.
DR PDBsum; 4Q1Q; -.
DR AlphaFoldDB; Q9XD84; -.
DR SMR; Q9XD84; -.
DR TCDB; 1.B.12.8.3; the autotransporter-1 (at-1) family.
DR PRIDE; Q9XD84; -.
DR EnsemblBacteria; CBJ01643; CBJ01643; ETEC_2141.
DR KEGG; elh:ETEC_2141; -.
DR HOGENOM; CLU_002318_0_0_6; -.
DR OMA; IMINNEM; -.
DR Proteomes; UP000006877; Chromosome.
DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:CACAO.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR Gene3D; 2.160.20.20; -; 1.
DR Gene3D; 2.40.128.130; -; 1.
DR InterPro; IPR030930; AIDA.
DR InterPro; IPR005546; Autotransporte_beta.
DR InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR InterPro; IPR012332; Autotransporter_pectin_lyase_C.
DR InterPro; IPR024973; ESPR.
DR InterPro; IPR006315; OM_autotransptr_brl.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR004899; Pertactin_central.
DR InterPro; IPR003991; Pertactin_virulence_factor.
DR Pfam; PF16168; AIDA; 3.
DR Pfam; PF03797; Autotransporter; 1.
DR Pfam; PF13018; ESPR; 1.
DR Pfam; PF03212; Pertactin; 1.
DR PRINTS; PR01484; PRTACTNFAMLY.
DR SMART; SM00869; Autotransporter; 1.
DR SUPFAM; SSF103515; SSF103515; 1.
DR SUPFAM; SSF51126; SSF51126; 2.
DR TIGRFAMs; TIGR01414; autotrans_barl; 1.
DR TIGRFAMs; TIGR04415; O_hepto_targRPT; 7.
DR PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell adhesion; Cell outer membrane;
KW Direct protein sequencing; Glycoprotein; Membrane; Periplasm; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane beta strand; Virulence.
FT SIGNAL 1..54
FT /evidence="ECO:0000269|PubMed:10417177,
FT ECO:0000269|PubMed:11119488"
FT CHAIN 55..989
FT /note="Adhesin/invasin TibA autotransporter"
FT /id="PRO_0000387584"
FT CHAIN 55..677
FT /note="Adhesin/invasin TibA"
FT /id="PRO_0000044607"
FT CHAIN 678..989
FT /note="Adhesin/invasin TibA translocator"
FT /id="PRO_0000044608"
FT REPEAT 82..100
FT /note="1-1"
FT REPEAT 101..119
FT /note="1-2"
FT REPEAT 120..138
FT /note="1-3"
FT REPEAT 139..157
FT /note="1-4"
FT REPEAT 158..176
FT /note="1-5"
FT REPEAT 177..195
FT /note="1-6"
FT REPEAT 196..214
FT /note="1-7"
FT REPEAT 215..233
FT /note="1-8"
FT REPEAT 234..251
FT /note="1-9"
FT REPEAT 252..270
FT /note="1-10"
FT REPEAT 271..289
FT /note="1-11"
FT REPEAT 290..308
FT /note="1-12"
FT REPEAT 639..643
FT /note="2-1"
FT REPEAT 644..648
FT /note="2-2"
FT REPEAT 649..653
FT /note="2-3"
FT REPEAT 654..658
FT /note="2-4"
FT REPEAT 659..663
FT /note="2-5"
FT REPEAT 664..668
FT /note="2-6"
FT REPEAT 669..673
FT /note="2-7"
FT REPEAT 674..678
FT /note="2-8"
FT DOMAIN 721..989
FT /note="Autotransporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00556"
FT REGION 82..308
FT /note="12 X 19 AA approximate repeats"
FT REGION 110..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..686
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 639..678
FT /note="8 X 5 AA repeats of P-[DG]-[AGT]-[DGA]-[NKT]"
FT STRAND 56..59
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 146..149
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 173..176
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 192..195
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 203..206
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 222..226
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 241..246
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 267..273
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 286..292
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 297..300
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 305..311
FT /evidence="ECO:0007829|PDB:4Q1Q"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:4Q1Q"
SQ SEQUENCE 989 AA; 101112 MW; 6A925466416E63BE CRC64;
MNKVYNTVWN ESTGTWVVTS ELTRKGGLRP RQIKRTVLAG LIAGLLMPSM PALAAAYDNQ
TIGRGETSKS MHLSAGDTAK NTTINSGGKQ YVSSGGSATS TTINIGGVQH VSSGGSATSS
TINSGGHQHV SSGGSATNTT VNNGGRQTVF SGGSAMGTII NSGGDQYVIS GGSATSASVT
SGARQFVSSG GIVKATSVNS GGRQYVRDGG SATDTVLNNT GRQFVSSGGS AAKTTINSGG
GMYLYGGSAT GTSIYNGGRQ YVSSGGSATN TTVYSGGRQH VYIDGNVTET TITSGGMLQV
EAGGSASKVI QNSGGAVITN TSAAVSGTND NGSFSIAGGS AVNMLLENGG YLTVFDGHQA
SDTMVGSDGT LDVRSGGVLY GTTTLTDKGA LVGDVVTNEG NLYYLNNSTA TFTGTLTGTG
TLTQEGGNTR FSGLLSQDGG IFLQSGGAMT MDALQAKANV TTQSGTTLTL DNGTILTGNV
AGDSTGAGDM AVKGASVWHL DGDSTVGALT LDNGTVDFRP STTTRMTPAF QAVSLALGSL
SGSGTFQMNT DIASHTGDML NVAGNASGNF VLDIKNTGLE PVSAGAPLQV VQTGGGDAAF
TLKGGKVDAG TWEYGLSKEN TNWYLKADTP PPVTPPTNPD ADNPDAGNPD AGNPDAGNPD
AGNPDAGKPG TGKPDAGTSS SPVRRTTKSV DAVLGMATAP AYVFNSELDN LRFRHGDVMQ
NTRAPGGVWG RYTGSDNRIS GGASSGYTLT QNGFETGADM VFDLSDSSLA VGTFFSYSDN
SIKHARGGKS NVDSSGGGLY ATWFDNDGYY VDGVLKYNRF NNELRTWMSD GTAVKGDYSQ
NGFGGSLEAG RTFSLNENAW AQPYVRTTAF RADKKEIRLN NGMKASIGAT KSLQAEAGLK
LGMTLDVAGK EVKPYLSAAV SHEFSDNNKV RINDTYDFRN DISGTTGKYG LGVNAQLTPN
AGVWAEARYE NGKQTESPIT GGVGFRINF
