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Protein

Glycosyltransferase TibC

Gene

tibC

Organism
Escherichia coli O78:H11 (strain H10407 / ETEC)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Glycosylates the TibA adhesin.1 Publication

GO - Molecular functioni

  • transferase activity, transferring glycosyl groups Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciECOL316401:GLD0-2180-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Glycosyltransferase TibC (EC:2.4.-.-)
Gene namesi
Name:tibC
Ordered Locus Names:ETEC_2140
OrganismiEscherichia coli O78:H11 (strain H10407 / ETEC)
Taxonomic identifieri316401 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000006877 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901E → K: No effect. 1 Publication
Mutagenesisi348 – 3481L → P: No effect. 1 Publication
Mutagenesisi358 – 3581C → R: Loss of glycosyltransferase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 406406Glycosyltransferase TibCPRO_0000076354Add
BLAST

Structurei

Secondary structure

1
406
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 193Combined sources
Helixi21 – 233Combined sources
Beta strandi25 – 284Combined sources
Beta strandi31 – 366Combined sources
Beta strandi41 – 477Combined sources
Turni48 – 503Combined sources
Beta strandi53 – 6513Combined sources
Beta strandi74 – 796Combined sources
Beta strandi81 – 855Combined sources
Beta strandi87 – 915Combined sources
Beta strandi98 – 1025Combined sources
Helixi108 – 12518Combined sources
Beta strandi128 – 1325Combined sources
Helixi135 – 1417Combined sources
Helixi142 – 1443Combined sources
Beta strandi148 – 1514Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi176 – 1805Combined sources
Helixi182 – 1854Combined sources
Turni187 – 1893Combined sources
Helixi190 – 1956Combined sources
Beta strandi218 – 2214Combined sources
Helixi228 – 2303Combined sources
Helixi237 – 24711Combined sources
Beta strandi251 – 2544Combined sources
Beta strandi259 – 2635Combined sources
Beta strandi266 – 2694Combined sources
Helixi283 – 2919Combined sources
Beta strandi294 – 2985Combined sources
Helixi303 – 3097Combined sources
Beta strandi314 – 3174Combined sources
Beta strandi319 – 3213Combined sources
Helixi323 – 3253Combined sources
Helixi342 – 3443Combined sources
Turni359 – 3635Combined sources
Turni365 – 3684Combined sources
Helixi369 – 3724Combined sources
Helixi376 – 39015Combined sources
Turni395 – 3973Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RAPX-ray2.88A/B/C/D/E/F/G/H/I/J/K/L1-406[»]
ProteinModelPortaliQ9S4K6.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

OMAiEFYTPWR.

Family and domain databases

InterProiIPR030929. Aah/TibC.
IPR002201. Glyco_trans_9.
[Graphical view]
PfamiPF01075. Glyco_transf_9. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04414. hepto_Aah_TibC. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9S4K6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTLKNTFFI TPPDTPTQAG PENIFYDFND GARVLLPEGK WHVRLLDADS
60 70 80 90 100
ENILFCCDVD KGWVTSSKKY FVRFRIQVFR QGEETPLLDE TLKLKDRPVL
110 120 130 140 150
ISFPTGTLGD LLGWFPYAER FQSLHKCRLE CTMSQDIIDL LAPQYPQIQF
160 170 180 190 200
STPDKPRTVA PYATYRVGLY FGGDTNNQPV DFRKVGFHRS AGYILGVDPR
210 220 230 240 250
EAPVRLDLSA PRVIQEPYVC IATQSTCQAK YWNNGTGWSE VIAHLKSLGY
260 270 280 290 300
RVMCIDRDAH YGQGFVWNHI PWGAEDFTGK LPLQERVNLL RHASFFIGLP
310 320 330 340 350
SGLSWLAWAT RIPVVLISGF SLPNSEFYTP WRVFNSHGCY GCWDDTSLNF
360 370 380 390 400
DHHDFLWCPR HKNTDRQFEC TRLITGAQVN GVINKLHRSL TEQGVEATLK

KGVSNE
Length:406
Mass (Da):46,325
Last modified:May 1, 2000 - v1
Checksum:i3FDDEA5C9D2FBDD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF131891 Genomic DNA. Translation: AAD46996.1.
FN649414 Genomic DNA. Translation: CBJ01642.1.
RefSeqiWP_000105682.1. NC_017633.1.

Genome annotation databases

EnsemblBacteriaiCBJ01642; CBJ01642; ETEC_2140.
KEGGielh:ETEC_2140.
PATRICi42960170. VBIEscCol136115_2452.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF131891 Genomic DNA. Translation: AAD46996.1.
FN649414 Genomic DNA. Translation: CBJ01642.1.
RefSeqiWP_000105682.1. NC_017633.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4RAPX-ray2.88A/B/C/D/E/F/G/H/I/J/K/L1-406[»]
ProteinModelPortaliQ9S4K6.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCBJ01642; CBJ01642; ETEC_2140.
KEGGielh:ETEC_2140.
PATRICi42960170. VBIEscCol136115_2452.

Phylogenomic databases

OMAiEFYTPWR.

Enzyme and pathway databases

BioCyciECOL316401:GLD0-2180-MONOMER.

Family and domain databases

InterProiIPR030929. Aah/TibC.
IPR002201. Glyco_trans_9.
[Graphical view]
PfamiPF01075. Glyco_transf_9. 1 hit.
[Graphical view]
TIGRFAMsiTIGR04414. hepto_Aah_TibC. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a glycoprotein produced by enterotoxigenic Escherichia coli."
    Lindenthal C., Elsinghorst E.A.
    Infect. Immun. 67:4084-4091(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: H10407 / ETEC.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: H10407 / ETEC.
  3. "Functional substitution of the TibC protein of enterotoxigenic Escherichia coli strains for the autotransporter adhesin heptosyltransferase of the AIDA system."
    Moormann C., Benz I., Schmidt M.A.
    Infect. Immun. 70:2264-2270(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-90; LEU-348 AND CYS-358.
    Strain: 469ST / ETEC, O128:H- / 147/1 / ETEC, O6:H- / 117/86 / ETEC and TX-1 / ETEC.

Entry informationi

Entry nameiTIBC_ECOH1
AccessioniPrimary (citable) accession number: Q9S4K6
Secondary accession number(s): E3PBM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: May 1, 2000
Last modified: July 22, 2015
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Able to functionally replace the autotransporter adhesin heptosyltransferase (AAH) of the AIDA system in fully restoring activity to the AIDA-I adhesin depending on the modification of AIDA with heptose residues.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.