Q9S4K6 · TIBC_ECOH1

Function

function

Glycosylates adhesin TibA (PubMed:11953358, PubMed:25310236).
Specifically adds anomer D-glycero-beta-D-manno-heptose (PubMed:25310236).
Can not use ADP-L-glycero-beta-D-manno-heptose as a sugar donnor (PubMed:25310236).

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-I with heptose residues.

Cofactor

Fe3+ (UniProtKB | Rhea| CHEBI:29034 )

Note: Binds 1 Fe3+ cation per subunit.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site107ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site108ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site109ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Active site110Proton acceptor
Binding site224ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site226ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site230ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site257ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site281ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site302ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site326ADP-D-glycero-beta-D-manno-heptose (UniProtKB | ChEBI)
Binding site339Fe3+ (UniProtKB | ChEBI); structural
Binding site342Fe3+ (UniProtKB | ChEBI); structural
Binding site358Fe3+ (UniProtKB | ChEBI); structural
Binding site370Fe3+ (UniProtKB | ChEBI); structural

GO annotations

AspectTerm
Molecular Functionglycosyltransferase activity
Molecular Functionmetal ion binding

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Autotransporter heptosyltransferase TibC
  • EC number

Gene names

    • Name
      tibC
    • Ordered locus names
      ETEC_2140

Organism names

Accessions

  • Primary accession
    Q9S4K6
  • Secondary accessions
    • E3PBM2

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis2-95Loss of catalytic activity.
Mutagenesis90No effect.
Mutagenesis110Loss of catalytic activity.
Mutagenesis230Loss of catalytic activity.
Mutagenesis265Loss of catalytic activity. Does not form homododecamer but forms homodimer.
Mutagenesis266Loss of catalytic activity. Does not form homododecamer but forms homodimer.
Mutagenesis286Severe loss of catalytic activity.
Mutagenesis300Loss of ligand stereospecificity. Can use both ADP-D,D-heptose and ADP-L,D-heptose as sugar donor.
Mutagenesis305Severe loss of catalytic activity.
Mutagenesis339Loss of catalytic activity. Loss of iron binding. Does not form homododecamer.
Mutagenesis342Loss of catalytic activity. Loss of iron binding. Does not form homododecamer.
Mutagenesis348No effect.
Mutagenesis358Loss of glycosyltransferase activity.
Mutagenesis358Loss of catalytic activity. Loss of iron binding. Does not form homododecamer.
Mutagenesis370Loss of catalytic activity. Loss of iron binding. Does not form homododecamer.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000763541-406Autotransporter heptosyltransferase TibC

Interaction

Subunit

Homododecamer composed of 6 homodimers forming a ring.

Family & Domains

Sequence similarities

Belongs to the glycosyltransferase 9 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    406
  • Mass (Da)
    46,325
  • Last updated
    2000-05-01 v1
  • Checksum
    3FDDEA5C9D2FBDD5
MSTLKNTFFITPPDTPTQAGPENIFYDFNDGARVLLPEGKWHVRLLDADSENILFCCDVDKGWVTSSKKYFVRFRIQVFRQGEETPLLDETLKLKDRPVLISFPTGTLGDLLGWFPYAERFQSLHKCRLECTMSQDIIDLLAPQYPQIQFSTPDKPRTVAPYATYRVGLYFGGDTNNQPVDFRKVGFHRSAGYILGVDPREAPVRLDLSAPRVIQEPYVCIATQSTCQAKYWNNGTGWSEVIAHLKSLGYRVMCIDRDAHYGQGFVWNHIPWGAEDFTGKLPLQERVNLLRHASFFIGLPSGLSWLAWATRIPVVLISGFSLPNSEFYTPWRVFNSHGCYGCWDDTSLNFDHHDFLWCPRHKNTDRQFECTRLITGAQVNGVINKLHRSLTEQGVEATLKKGVSNE

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF131891
EMBL· GenBank· DDBJ
AAD46996.1
EMBL· GenBank· DDBJ
Genomic DNA
FN649414
EMBL· GenBank· DDBJ
CBJ01642.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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