TIBC_ECOH1
ID TIBC_ECOH1 Reviewed; 406 AA.
AC Q9S4K6; E3PBM2;
DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Glycosyltransferase TibC;
DE EC=2.4.-.-;
GN Name=tibC; OrderedLocusNames=ETEC_2140;
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].
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 FUNCTION, AND MUTAGENESIS OF GLU-90; LEU-348 AND CYS-358.
RC STRAIN=469ST / ETEC, O128:H- / 147/1 / ETEC, O6:H- / 117/86 / ETEC, and
RC TX-1 / ETEC;
RX PubMed=11953358; DOI=10.1128/iai.70.5.2264-2270.2002;
RA Moormann C., Benz I., Schmidt M.A.;
RT "Functional substitution of the TibC protein of enterotoxigenic Escherichia
RT coli strains for the autotransporter adhesin heptosyltransferase of the
RT AIDA system.";
RL Infect. Immun. 70:2264-2270(2002).
CC -!- FUNCTION: Glycosylates the TibA adhesin. {ECO:0000269|PubMed:11953358}.
CC -!- MISCELLANEOUS: Able to functionally replace the autotransporter adhesin
CC heptosyltransferase (AAH) of the AIDA system in fully restoring
CC activity to the AIDA-I adhesin depending on the modification of AIDA
CC with heptose residues.
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DR EMBL; AF131891; AAD46996.1; -; Genomic_DNA.
DR EMBL; FN649414; CBJ01642.1; -; Genomic_DNA.
DR RefSeq; WP_000105682.1; NC_017633.1.
DR PDB; 4RAP; X-ray; 2.88 A; A/B/C/D/E/F/G/H/I/J/K/L=1-406.
DR PDBsum; 4RAP; -.
DR AlphaFoldDB; Q9S4K6; -.
DR SMR; Q9S4K6; -.
DR PRIDE; Q9S4K6; -.
DR EnsemblBacteria; CBJ01642; CBJ01642; ETEC_2140.
DR KEGG; elh:ETEC_2140; -.
DR HOGENOM; CLU_044689_0_0_6; -.
DR OMA; EFYTPWR; -.
DR Proteomes; UP000006877; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:CACAO.
DR CDD; cd03789; GT9_LPS_heptosyltransferase; 1.
DR InterPro; IPR030929; Aah/TibC.
DR InterPro; IPR002201; Glyco_trans_9.
DR Pfam; PF01075; Glyco_transf_9; 1.
DR TIGRFAMs; TIGR04414; hepto_Aah_TibC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Transferase.
FT CHAIN 1..406
FT /note="Glycosyltransferase TibC"
FT /id="PRO_0000076354"
FT MUTAGEN 90
FT /note="E->K: No effect."
FT /evidence="ECO:0000269|PubMed:11953358"
FT MUTAGEN 348
FT /note="L->P: No effect."
FT /evidence="ECO:0000269|PubMed:11953358"
FT MUTAGEN 358
FT /note="C->R: Loss of glycosyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11953358"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 25..28
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 31..36
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4RAP"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 53..65
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 108..125
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 128..132
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 135..141
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 148..151
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4RAP"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 190..195
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 218..221
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 237..247
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 251..254
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 283..291
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 303..309
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 314..317
FT /evidence="ECO:0007829|PDB:4RAP"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 342..344
FT /evidence="ECO:0007829|PDB:4RAP"
FT TURN 359..363
FT /evidence="ECO:0007829|PDB:4RAP"
FT TURN 365..368
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 369..372
FT /evidence="ECO:0007829|PDB:4RAP"
FT HELIX 376..390
FT /evidence="ECO:0007829|PDB:4RAP"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:4RAP"
SQ SEQUENCE 406 AA; 46325 MW; 3FDDEA5C9D2FBDD5 CRC64;
MSTLKNTFFI TPPDTPTQAG PENIFYDFND GARVLLPEGK WHVRLLDADS ENILFCCDVD
KGWVTSSKKY FVRFRIQVFR QGEETPLLDE TLKLKDRPVL ISFPTGTLGD LLGWFPYAER
FQSLHKCRLE CTMSQDIIDL LAPQYPQIQF STPDKPRTVA PYATYRVGLY FGGDTNNQPV
DFRKVGFHRS AGYILGVDPR EAPVRLDLSA PRVIQEPYVC IATQSTCQAK YWNNGTGWSE
VIAHLKSLGY RVMCIDRDAH YGQGFVWNHI PWGAEDFTGK LPLQERVNLL RHASFFIGLP
SGLSWLAWAT RIPVVLISGF SLPNSEFYTP WRVFNSHGCY GCWDDTSLNF DHHDFLWCPR
HKNTDRQFEC TRLITGAQVN GVINKLHRSL TEQGVEATLK KGVSNE