Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase

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P76473 (ARNT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
EC=2.4.2.43

Alternative name(s):
4-amino-4-deoxy-L-arabinose lipid A transferase
Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase
Polymyxin resistance protein PmrK
Undecaprenyl phosphate-alpha-L-Ara4N transferase

Gene names

Name:	arnT
Synonyms:	pmrK, yfbI
Ordered Locus Names:	b2257, JW2251

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	550 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the transfer of the L-Ara4N moiety of the glycolipid undecaprenyl phosphate-alpha-L-Ara4N to lipid A. The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides. Ref.3
Catalytic activity	4-amino-4-deoxy-alpha-L-arabinopyranosyl di-trans,octa-cis-undecaprenyl phosphate + lipid IV(A) = lipid II(A) + di-trans,octa-cis-undecaprenyl phosphate. Ref.3
Pathway	Lipopolysaccharide metabolism; 4-amino-4-deoxy-beta-L-arabinose-lipid A biosynthesis. HAMAP-Rule MF_01165
Subcellular location	Cell inner membrane; Multi-pass membrane protein Ref.4.
Induction	Induced by BasR By similarity.
Sequence similarities	Belongs to the glycosyltransferase 83 family.

Ontologies

Keywords
Biological process	Lipid A biosynthesis Lipid biosynthesis Lipid metabolism Lipopolysaccharide biosynthesis
Cellular component	Cell inner membrane Cell membrane Membrane
Domain	Transmembrane Transmembrane helix
Molecular function	Glycosyltransferase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	lipid A biosynthetic process Inferred from electronic annotation. Source: HAMAP lipopolysaccharide biosynthetic process Inferred from mutant phenotype PubMed 11535605. Source: EcoCyc protein O-linked glycosylation Inferred from electronic annotation. Source: InterPro response to iron(III) ion Inferred from genetic interaction PubMed 12139617. Source: EcoCyc
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	mannosyltransferase activity Inferred from electronic annotation. Source: InterPro transferase activity, transferring pentosyl groups Inferred from mutant phenotype PubMed 17928292. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 550

550

Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase HAMAP-Rule MF_01165

PRO_0000121504

Regions

Transmembrane

7 – 27

Helical; Potential

Transmembrane

81 – 101

Helical; Potential

Transmembrane

110 – 131

Helical; Potential

Transmembrane

137 – 154

Helical; Potential

Transmembrane

165 – 185

Helical; Potential

Transmembrane

204 – 224

Helical; Potential

Transmembrane

255 – 275

Helical; Potential

Transmembrane

288 – 308

Helical; Potential

Transmembrane

315 – 335

Helical; Potential

Transmembrane

346 – 366

Helical; Potential

Transmembrane

383 – 403

Helical; Potential

Transmembrane

406 – 426

Helical; Potential

Sequences

Sequence

Length

Mass (Da)

Tools

P76473 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E57E0C3A0608D745
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FASTA

550

62,543

        10         20         30         40         50         60 
MKSVRYLIGL FAFIACYYLL PISTRLLWQP DETRYAEISR EMLASGDWIV PHLLGLRYFE 

        70         80         90        100        110        120 
KPIAGYWINS IGQWLFGANN FGVRAGVIFA TLLTAALVTW FTLRLWRDKR LALLATVIYL 

       130        140        150        160        170        180 
SLFIVYAIGT YAVLDPFIAF WLVAGMCSFW LAMQAQTWKG KSAGFLLLGI TCGMGVMTKG 

       190        200        210        220        230        240 
FLALAVPVLS VLPWVATQKR WKDLFIYGWL AVISCVLTVL PWGLAIAQRE PNFWHYFFWV 

       250        260        270        280        290        300 
EHIQRFALDD AQHRAPFWYY VPVIIAGSLP WLGLLPGALY TGWKNRKHSA TVYLLSWTIM 

       310        320        330        340        350        360 
PLLFFSVAKG KLPTYILSCF ASLAMLMAHY ALLAAKNNPL ALRINGWINI AFGVTGIIAT 

       370        380        390        400        410        420 
FVVSPWGPMN TPVWQTFESY KVFCAWSIFS LWAFFGWYTL TNVEKTWPFA ALCPLGLALL 

       430        440        450        460        470        480 
VGFSIPDRVM EGKHPQFFVE MTQESLQPSR YILTDSVGVA AGLAWSLQRD DIIMYRQTGE 

       490        500        510        520        530        540 
LKYGLNYPDA KGRFVSGDEF ANWLNQHRQE GIITLVLSVD RDEDINSLAI PPADAIDRQE 

       550 
RLVLIQYRPK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"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.
[3]	"An inner membrane enzyme in Salmonella and Escherichia coli that transfers 4-amino-4-deoxy-L-arabinose to lipid A: induction on polymyxin-resistant mutants and role of a novel lipid-linked donor." Trent M.S., Ribeiro A.A., Lin S., Cotter R.J., Raetz C.R.H. J. Biol. Chem. 276:43122-43131(2001) [PubMed] [Europe PMC] [Abstract] Cited for: CATALYTIC ACTIVITY, FUNCTION. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"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: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U00096 Genomic DNA. Translation: AAC75317.1. AP009048 Genomic DNA. Translation: BAE76674.1.
PIR	G64996.
RefSeq	NP_416760.1. NC_000913.2. YP_490496.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P76473.
ModBase	Search...
Protein-protein interaction databases
STRING	511145.b2257.
Protein family/group databases
CAZy	GT83. Glycosyltransferase Family 83.
Proteomic databases
PRIDE	P76473.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC75317; AAC75317; b2257. BAE76674; BAE76674; BAE76674.
GeneID	12931505. 947297.
KEGG	ecj:Y75_p2220. eco:b2257.
PATRIC	32119879. VBIEscCol129921_2349.
Organism-specific databases
EchoBASE	EB3846.
EcoGene	EG14093. arnT.
Phylogenomic databases
eggNOG	COG1807.
HOGENOM	HOG000273002.
KO	K07264.
OMA	RFAMDDA.
ProtClustDB	PRK13279.
Enzyme and pathway databases
BioCyc	EcoCyc:G7170-MONOMER. ECOL316407:JW2251-MONOMER. MetaCyc:G7170-MONOMER.
UniPathway	UPA00037.
Gene expression databases
Genevestigator	P76473.
Family and domain databases
HAMAP	MF_01165. ArnT_transfer.
InterPro	IPR022839. ArnT_tfrase. IPR003342. Glyco_trans_39. [Graphical view]
Pfam	PF02366. PMT. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARNT_ECOLI

Accession

Primary (citable) accession number: P76473
Secondary accession number(s): Q2MAN2

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 2001
Last sequence update:	February 1, 1997
Last modified:	May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic 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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents