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P27243 (RFAL_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
O-antigen ligase
Gene names
Name:rfaL
Synonyms:waaL
Ordered Locus Names:b3622, JW3597
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Adds the O-antigen on the glucose group of LPS.

Pathway

Bacterial outer membrane biogenesis; LPS core biosynthesis.

Subcellular location

Cell inner membrane; Multi-pass membrane protein.

Ontologies

Keywords
   Biological processLipopolysaccharide biosynthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processlipopolysaccharide core region biosynthetic process

Inferred from mutant phenotype PubMed 1385388. Source: EcoCyc

   Cellular_componentintegral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionO antigen ligase activity

Inferred from genetic interaction PubMed 1385388. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419O-antigen ligase
PRO_0000097284

Regions

Topological domain1 – 1717Cytoplasmic Potential
Transmembrane18 – 3821Helical; Potential
Topological domain391Periplasmic Potential
Transmembrane40 – 6021Helical; Potential
Topological domain61 – 7111Cytoplasmic Potential
Transmembrane72 – 9221Helical; Potential
Topological domain93 – 10513Periplasmic Potential
Transmembrane106 – 12621Helical; Potential
Topological domain127 – 1359Cytoplasmic Potential
Transmembrane136 – 15621Helical; Potential
Topological domain157 – 16812Periplasmic Potential
Transmembrane169 – 18921Helical; Potential
Topological domain190 – 1934Cytoplasmic Potential
Transmembrane194 – 21421Helical; Potential
Topological domain2151Periplasmic Potential
Transmembrane216 – 23621Helical; Potential
Topological domain237 – 2415Cytoplasmic Potential
Transmembrane242 – 26221Helical; Potential
Topological domain263 – 34684Periplasmic Potential
Transmembrane347 – 36721Helical; Potential
Topological domain368 – 3692Cytoplasmic Potential
Transmembrane370 – 39021Helical; Potential
Transmembrane391 – 41121Helical; Potential
Topological domain412 – 4198Cytoplasmic Potential

Experimental info

Sequence conflict205 – 22420VLYVL…LFPII → GTLCSGANTNQSNPTPVPYN in AAA24524. Ref.1
Sequence conflict3071R → T in AAA24524. Ref.1
Sequence conflict3441A → R in AAA24524. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P27243 [UniParc].

Last modified August 29, 2003. Version 2.
Checksum: E15382BD2CC70533

FASTA41946,878
        10         20         30         40         50         60 
MLTSFKLHSL KPYTLKSSMI LEIITYILCF FSMIIAFVDN TFSIKIYNIT AIVCLLSLIL 

        70         80         90        100        110        120 
RGRQENYNIK NLILPLSIFL IGLLDLIWYS AFKVDNSPFR ATYHSYLNTA KIFIFGSFIV 

       130        140        150        160        170        180 
FLTLTSQLKS KKESVLYTLY SLSFLIAGYA MYINSIHEND RISFGVGTAT GAAYSTMLIG 

       190        200        210        220        230        240 
IVSGVAILYT KKNHPFLFLL NSCAVLYVLA LTQTRATLLL FPIICVAALI AYYNKSPKKF 

       250        260        270        280        290        300 
TSSIVLLIAI LASIVIIFNK PIQNRYNEAL NDLNSYTNAN SVTSLGARLA MYEIGLNIFI 

       310        320        330        340        350        360 
KSPFSFRSAE SRAESMNLLV AEHNRLRGAL EFSNVHLHNE IIEAGSLKGL MGIFSTLFLY 

       370        380        390        400        410 
FSLFYIAYKK RALGLLILTL GIVGIGLSDV IIWARSIPII IISAIVLLLV INNRNNTIN

« Hide

References

« Hide 'large scale' references
[1]"Comparison of lipopolysaccharide biosynthesis genes rfaK, rfaL, rfaY, and rfaZ of Escherichia coli K-12 and Salmonella typhimurium."
Klena J.D., Pradel E., Schnaitman C.A.
J. Bacteriol. 174:4746-4752(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"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.
[5]"Global topology analysis of the Escherichia coli inner membrane proteome."
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.
Science 308:1321-1323(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: TOPOLOGY [LARGE SCALE ANALYSIS].
Strain: K12 / MG1655 / ATCC 47076.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M95398 Genomic DNA. Translation: AAA24524.1.
U00039 Genomic DNA. Translation: AAB18599.1.
U00096 Genomic DNA. Translation: AAC76646.1.
AP009048 Genomic DNA. Translation: BAE77670.1.
PIRS47843.
RefSeqNP_418079.1. NC_000913.2.
YP_491811.1. NC_007779.1.

3D structure databases

ProteinModelPortalP27243.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10673N.
IntActP27243. 1 interaction.
MINTMINT-1286025.
STRING511145.b3622.

Protein family/group databases

TCDB9.B.67.5.1. putative inorganic carbon (HCO3-) transporter/O-antigen polymerase (ICT/OAP) family.

Proteomic databases

PRIDEP27243.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76646; AAC76646; b3622.
BAE77670; BAE77670; BAE77670.
GeneID12934304.
948148.
KEGGecj:Y75_p3552.
eco:b3622.
PATRIC32122731. VBIEscCol129921_3742.

Organism-specific databases

EchoBASEEB1394.
EcoGeneEG11424. rfaL.

Phylogenomic databases

eggNOGCOG3307.
HOGENOMHOG000054845.
KOK02847.
OMATVHMHNE.
ProtClustDBCLSK2752733.

Enzyme and pathway databases

BioCycEcoCyc:EG11424-MONOMER.
ECOL316407:JW3597-MONOMER.
MetaCyc:EG11424-MONOMER.
UniPathwayUPA00958.

Gene expression databases

GenevestigatorP27243.

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameRFAL_ECOLI
AccessionPrimary (citable) accession number: P27243
Secondary accession number(s): Q2M7T6
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 29, 2003
Last modified: May 1, 2013
This is version 104 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents