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Protein

Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase

Gene

arnC

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

Functioni

Catalyzes the transfer of 4-deoxy-4-formamido-L-arabinose from UDP to undecaprenyl phosphate. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.1 Publication

Catalytic activityi

UDP-4-deoxy-4-formamido-beta-L-arabinose + ditrans,octacis-undecaprenyl phosphate = UDP + 4-deoxy-4-formamido-alpha-L-arabinose ditrans,octacis-undecaprenyl phosphate.1 Publication

Pathwayi: 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose and undecaprenyl phosphate.1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase (arnC)
  2. Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD (arnD)
This subpathway is part of the pathway 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis, which is itself part of Glycolipid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate from UDP-4-deoxy-4-formamido-beta-L-arabinose and undecaprenyl phosphate, the pathway 4-amino-4-deoxy-alpha-L-arabinose undecaprenyl phosphate biosynthesis and in Glycolipid biosynthesis.

Pathwayi: lipopolysaccharide biosynthesis

This protein is involved in the pathway lipopolysaccharide biosynthesis, which is part of Bacterial outer membrane biogenesis.1 Publication
View all proteins of this organism that are known to be involved in the pathway lipopolysaccharide biosynthesis and in Bacterial outer membrane biogenesis.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Antibiotic resistance, Lipid A biosynthesis, Lipid biosynthesis, Lipid metabolism, Lipopolysaccharide biosynthesis

Enzyme and pathway databases

BioCyciEcoCyc:G7167-MONOMER.
ECOL316407:JW2248-MONOMER.
MetaCyc:G7167-MONOMER.
UniPathwayiUPA00030.
UPA00036; UER00495.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.2.1.8. the glycosyl transferase 2 (gt2) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase (EC:2.4.2.53)
Alternative name(s):
Polymyxin resistance protein PmrF
Undecaprenyl-phosphate Ara4FN transferase
Short name:
Ara4FN transferase
Gene namesi
Name:arnC
Synonyms:pmrF, yfbF
Ordered Locus Names:b2254, JW2248
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG14090. arnC.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 235235CytoplasmicSequence analysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence analysisAdd
BLAST
Topological domaini257 – 26913PeriplasmicSequence analysisAdd
BLAST
Transmembranei270 – 29021HelicalSequence analysisAdd
BLAST
Topological domaini291 – 32232CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of membrane Source: UniProtKB-KW
  • membrane Source: EcoCyc
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 322322Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferasePRO_0000059195Add
BLAST

Proteomic databases

EPDiP77757.
PaxDbiP77757.

Expressioni

Inductioni

Induced by BasR.By similarity

Interactioni

Protein-protein interaction databases

BioGridi4260496. 313 interactions.
IntActiP77757. 3 interactions.
STRINGi511145.b2254.

Structurei

3D structure databases

ProteinModelPortaliP77757.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyltransferase 2 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105CKK. Bacteria.
COG0463. LUCA.
HOGENOMiHOG000283251.
InParanoidiP77757.
KOiK10012.
OMAiHESQKRP.
OrthoDBiEOG64FKGS.
PhylomeDBiP77757.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01164. ArnC_transfer.
InterProiIPR022857. ArnC_tfrase.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.

Sequencei

Sequence statusi: Complete.

P77757-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFEIHPVKKV SVVIPVYNEQ ESLPELIRRT TTACESLGKE YEILLIDDGS
60 70 80 90 100
SDNSAHMLVE ASQAENSHIV SILLNRNYGQ HSAIMAGFSH VTGDLIITLD
110 120 130 140 150
ADLQNPPEEI PRLVAKADEG YDVVGTVRQN RQDSWFRKTA SKMINRLIQR
160 170 180 190 200
TTGKAMGDYG CMLRAYRRHI VDAMLHCHER STFIPILANI FARRAIEIPV
210 220 230 240 250
HHAEREFGES KYSFMRLINL MYDLVTCLTT TPLRMLSLLG SIIAIGGFSI
260 270 280 290 300
AVLLVILRLT FGPQWAAEGV FMLFAVLFTF IGAQFIGMGL LGEYIGRIYT
310 320
DVRARPRYFV QQVIRPSSKE NE
Length:322
Mass (Da):36,339
Last modified:February 1, 1997 - v1
Checksum:i4E293C24969C2679
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ011863 Genomic DNA. Translation: AAY34350.1.
U00096 Genomic DNA. Translation: AAC75314.1.
AP009048 Genomic DNA. Translation: BAA16077.1.
PIRiD64996.
RefSeqiNP_416757.1. NC_000913.3.
WP_000461657.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75314; AAC75314; b2254.
BAA16077; BAA16077; BAA16077.
GeneIDi945275.
KEGGiecj:JW2248.
eco:b2254.
PATRICi32119873. VBIEscCol129921_2346.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ011863 Genomic DNA. Translation: AAY34350.1.
U00096 Genomic DNA. Translation: AAC75314.1.
AP009048 Genomic DNA. Translation: BAA16077.1.
PIRiD64996.
RefSeqiNP_416757.1. NC_000913.3.
WP_000461657.1. NZ_LN832404.1.

3D structure databases

ProteinModelPortaliP77757.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260496. 313 interactions.
IntActiP77757. 3 interactions.
STRINGi511145.b2254.

Protein family/group databases

CAZyiGT2. Glycosyltransferase Family 2.
TCDBi4.D.2.1.8. the glycosyl transferase 2 (gt2) family.

Proteomic databases

EPDiP77757.
PaxDbiP77757.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75314; AAC75314; b2254.
BAA16077; BAA16077; BAA16077.
GeneIDi945275.
KEGGiecj:JW2248.
eco:b2254.
PATRICi32119873. VBIEscCol129921_2346.

Organism-specific databases

EchoBASEiEB3843.
EcoGeneiEG14090. arnC.

Phylogenomic databases

eggNOGiENOG4105CKK. Bacteria.
COG0463. LUCA.
HOGENOMiHOG000283251.
InParanoidiP77757.
KOiK10012.
OMAiHESQKRP.
OrthoDBiEOG64FKGS.
PhylomeDBiP77757.

Enzyme and pathway databases

UniPathwayiUPA00030.
UPA00036; UER00495.
BioCyciEcoCyc:G7167-MONOMER.
ECOL316407:JW2248-MONOMER.
MetaCyc:G7167-MONOMER.

Miscellaneous databases

PROiP77757.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_01164. ArnC_transfer.
InterProiIPR022857. ArnC_tfrase.
IPR001173. Glyco_trans_2-like.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF00535. Glycos_transf_2. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A formyltransferase required for polymyxin resistance in Escherichia coli and the modification of lipid A with 4-amino-4-deoxy-L-arabinose: identification and function of UDP-4-deoxy-4-formamido-L-arabinose."
    Breazeale S.D., Ribeiro A.A., McClerren A.L., Raetz C.R.H.
    J. Biol. Chem. 280:14154-14167(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBSTRATE SPECIFICITY, CATALYTIC ACTIVITY.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  2. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
    Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
    , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
    DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. 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. "Oxidative decarboxylation of UDP-glucuronic acid in extracts of polymyxin-resistant Escherichia coli. Origin of lipid A species modified with 4-amino-4-deoxy-L-arabinose."
    Breazeale S.D., Ribeiro A.A., Raetz C.R.H.
    J. Biol. Chem. 277:2886-2896(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  6. "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.
  7. "An undecaprenyl phosphate-aminoarabinose flippase required for polymyxin resistance in Escherichia coli."
    Yan A., Guan Z., Raetz C.R.H.
    J. Biol. Chem. 282:36077-36089(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PATHWAY.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

Entry informationi

Entry nameiARNC_ECOLI
AccessioniPrimary (citable) accession number: P77757
Secondary accession number(s): P78179, Q4U4N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 126 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

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. 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.