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Protein

ADP-heptose--LPS heptosyltransferase 2

Gene

rfaF

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Pathwayi: LPS core biosynthesis

This protein is involved in the pathway LPS core biosynthesis, which is part of Bacterial outer membrane biogenesis.
View all proteins of this organism that are known to be involved in the pathway LPS core biosynthesis and in Bacterial outer membrane biogenesis.

GO - Molecular functioni

  • ADP-heptose-lipopolysaccharide heptosyltransferase activity Source: CACAO
  • transferase activity, transferring glycosyl groups Source: EcoCyc

GO - Biological processi

  • lipopolysaccharide core region biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:EG12210-MONOMER.
ECOL316407:JW3595-MONOMER.
MetaCyc:EG12210-MONOMER.
BRENDAi2.4.99.B7. 2026.
UniPathwayiUPA00958.

Protein family/group databases

CAZyiGT9. Glycosyltransferase Family 9.

Names & Taxonomyi

Protein namesi
Recommended name:
ADP-heptose--LPS heptosyltransferase 2 (EC:2.-.-.-)
Alternative name(s):
ADP-heptose--LPS heptosyltransferase II
Gene namesi
Name:rfaF
Synonyms:waaF
Ordered Locus Names:b3620, JW3595
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12210. rfaF.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348ADP-heptose--LPS heptosyltransferase 2PRO_0000207262Add
BLAST

Proteomic databases

EPDiP37692.
PaxDbiP37692.
PRIDEiP37692.

Interactioni

Protein-protein interaction databases

BioGridi4263306. 335 interactions.
DIPiDIP-10667N.
IntActiP37692. 11 interactions.
STRINGi511145.b3620.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 65Combined sources
Helixi11 – 2717Combined sources
Beta strandi32 – 376Combined sources
Helixi39 – 413Combined sources
Helixi42 – 454Combined sources
Beta strandi51 – 566Combined sources
Helixi66 – 7510Combined sources
Turni76 – 805Combined sources
Beta strandi82 – 865Combined sources
Helixi92 – 943Combined sources
Helixi95 – 995Combined sources
Beta strandi103 – 1086Combined sources
Turni110 – 1123Combined sources
Turni114 – 1163Combined sources
Beta strandi119 – 1213Combined sources
Turni125 – 1273Combined sources
Helixi131 – 1377Combined sources
Helixi142 – 1443Combined sources
Helixi148 – 1503Combined sources
Helixi164 – 17310Combined sources
Beta strandi178 – 1803Combined sources
Beta strandi182 – 1865Combined sources
Helixi193 – 1953Combined sources
Helixi199 – 21113Combined sources
Beta strandi215 – 2184Combined sources
Helixi222 – 2243Combined sources
Helixi225 – 2328Combined sources
Helixi237 – 2404Combined sources
Beta strandi243 – 2453Combined sources
Turni247 – 2493Combined sources
Helixi252 – 2609Combined sources
Beta strandi262 – 2709Combined sources
Helixi271 – 2788Combined sources
Beta strandi283 – 2908Combined sources
Beta strandi302 – 3087Combined sources
Helixi325 – 3284Combined sources
Helixi332 – 34716Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PSWX-ray2.00A1-348[»]
ProteinModelPortaliP37692.
SMRiP37692. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37692.

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 9 family.Curated

Phylogenomic databases

eggNOGiENOG4105XA0. Bacteria.
COG0859. LUCA.
HOGENOMiHOG000237541.
InParanoidiP37692.
KOiK02843.
OMAiCLKQRHP.
OrthoDBiEOG64N9TX.
PhylomeDBiP37692.

Family and domain databases

InterProiIPR002201. Glyco_trans_9.
IPR011910. LipoPS_heptosylTferase-II.
[Graphical view]
PfamiPF01075. Glyco_transf_9. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02195. heptsyl_trn_II. 1 hit.

Sequencei

Sequence statusi: Complete.

P37692-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKILVIGPSW VGDMMMSQSL YRTLQARYPQ AIIDVMAPAW CRPLLSRMPE
60 70 80 90 100
VNEAIPMPLG HGALEIGERR KLGHSLREKR YDRAYVLPNS FKSALVPFFA
110 120 130 140 150
GIPHRTGWRG EMRYGLLNDV RVLDKEAWPL MVERYIALAY DKGIMRTAQD
160 170 180 190 200
LPQPLLWPQL QVSEGEKSYT CNQFSLSSER PMIGFCPGAE FGPAKRWPHY
210 220 230 240 250
HYAELAKQLI DEGYQVVLFG SAKDHEAGNE ILAALNTEQQ AWCRNLAGET
260 270 280 290 300
QLDQAVILIA ACKAIVTNDS GLMHVAAALN RPLVALYGPS SPDFTPPLSH
310 320 330 340
KARVIRLITG YHKVRKGDAA EGYHQSLIDI TPQRVLEELN ALLLQEEA
Length:348
Mass (Da):39,042
Last modified:October 1, 1994 - v1
Checksum:iC5F57BC94B15BA6A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161Missing in M33577 (PubMed:2198271).Curated
Sequence conflicti19 – 202SL → DR in M33577 (PubMed:2198271).Curated
Sequence conflicti105 – 1051R → S (PubMed:8478319).Curated
Sequence conflicti151 – 1511L → R (PubMed:8478319).Curated
Sequence conflicti159 – 1591Q → H (PubMed:8478319).Curated
Sequence conflicti204 – 2052EL → DV (PubMed:8478319).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18597.1.
U00096 Genomic DNA. Translation: AAC76644.1.
AP009048 Genomic DNA. Translation: BAE77672.1.
M33577 Genomic DNA. No translation available.
X62530 Genomic DNA. No translation available.
PIRiS47841.
RefSeqiNP_418077.1. NC_000913.3.
WP_000699219.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76644; AAC76644; b3620.
BAE77672; BAE77672; BAE77672.
GeneIDi948135.
KEGGiecj:JW3595.
eco:b3620.
PATRICi32122727. VBIEscCol129921_3740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U00039 Genomic DNA. Translation: AAB18597.1.
U00096 Genomic DNA. Translation: AAC76644.1.
AP009048 Genomic DNA. Translation: BAE77672.1.
M33577 Genomic DNA. No translation available.
X62530 Genomic DNA. No translation available.
PIRiS47841.
RefSeqiNP_418077.1. NC_000913.3.
WP_000699219.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PSWX-ray2.00A1-348[»]
ProteinModelPortaliP37692.
SMRiP37692. Positions 1-348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263306. 335 interactions.
DIPiDIP-10667N.
IntActiP37692. 11 interactions.
STRINGi511145.b3620.

Protein family/group databases

CAZyiGT9. Glycosyltransferase Family 9.

Proteomic databases

EPDiP37692.
PaxDbiP37692.
PRIDEiP37692.

Protocols and materials databases

DNASUi948135.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76644; AAC76644; b3620.
BAE77672; BAE77672; BAE77672.
GeneIDi948135.
KEGGiecj:JW3595.
eco:b3620.
PATRICi32122727. VBIEscCol129921_3740.

Organism-specific databases

EchoBASEiEB2124.
EcoGeneiEG12210. rfaF.

Phylogenomic databases

eggNOGiENOG4105XA0. Bacteria.
COG0859. LUCA.
HOGENOMiHOG000237541.
InParanoidiP37692.
KOiK02843.
OMAiCLKQRHP.
OrthoDBiEOG64N9TX.
PhylomeDBiP37692.

Enzyme and pathway databases

UniPathwayiUPA00958.
BioCyciEcoCyc:EG12210-MONOMER.
ECOL316407:JW3595-MONOMER.
MetaCyc:EG12210-MONOMER.
BRENDAi2.4.99.B7. 2026.

Miscellaneous databases

EvolutionaryTraceiP37692.
PROiP37692.

Family and domain databases

InterProiIPR002201. Glyco_trans_9.
IPR011910. LipoPS_heptosylTferase-II.
[Graphical view]
PfamiPF01075. Glyco_transf_9. 1 hit.
[Graphical view]
TIGRFAMsiTIGR02195. heptsyl_trn_II. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
    Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
    Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Cloning, expression, and characterization of the Escherichia coli K-12 rfaD gene."
    Pegues J.C., Chen L., Gordon A.W., Ding L., Coleman W.G. Jr.
    J. Bacteriol. 172:4652-4660(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51.
    Strain: K12.
  5. "Cloning and characterization of the Escherichia coli K-12 rfa-2 (rfaC) gene, a gene required for lipopolysaccharide inner core synthesis."
    Chen L., Coleman W.G. Jr.
    J. Bacteriol. 175:2534-2540(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 52-348.
    Strain: K12.

Entry informationi

Entry nameiRFAF_ECOLI
AccessioniPrimary (citable) accession number: P37692
Secondary accession number(s): Q2M7T4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: March 16, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.