Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q4K884 (ARNT2_PSEF5) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 56. Feed History...

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

Names and origin

Protein namesRecommended name:
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 2
EC=2.4.2.43
Alternative name(s):
4-amino-4-deoxy-L-arabinose lipid A transferase 2
Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase
Undecaprenyl phosphate-alpha-L-Ara4N transferase 2
Gene names
Name:arnT2
Ordered Locus Names:PFL_4461
OrganismPseudomonas fluorescens (strain Pf-5 / ATCC BAA-477) [Complete proteome] [HAMAP]
Taxonomic identifier220664 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas ›

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity. HAMAP-Rule MF_01165

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. HAMAP-Rule MF_01165

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 By similarity HAMAP-Rule MF_01165.

Sequence similarities

Belongs to the glycosyltransferase 83 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 583583Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 2 HAMAP-Rule MF_01165
PRO_0000380020

Regions

Transmembrane42 – 6221Helical; Potential
Transmembrane113 – 13523Helical; Potential
Transmembrane145 – 16521Helical; Potential
Transmembrane166 – 18621Helical; Potential
Transmembrane209 – 22921Helical; Potential
Transmembrane241 – 26121Helical; Potential
Transmembrane290 – 31021Helical; Potential
Transmembrane321 – 34121Helical; Potential
Transmembrane345 – 36521Helical; Potential
Transmembrane380 – 40021Helical; Potential
Transmembrane409 – 42921Helical; Potential
Transmembrane440 – 46021Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
Q4K884 [UniParc].

Last modified August 2, 2005. Version 1.
Checksum: F9231E122AABDCED

FASTA58365,170
        10         20         30         40         50         60 
MTSRIQMHRT SPPPAYGTSA PPSGFTLGAS TTSTLQRWAL PLLLVAFGLF YLLPLTSHGL 

        70         80         90        100        110        120 
WIPDETRYAQ ISQEMLLSGD WVAPHFMGIR YFEKPIAGYW LIAIGQAVFG DNLFGVRIAS 

       130        140        150        160        170        180 
ALSTGLSVLL AYLITRRMWN DPRKSFAAAL LYMSFGLIAG QAGYSNLDPQ FTLWVNLSLV 

       190        200        210        220        230        240 
ALWFALDGRS TRERLLAWAG LGVACGMGFM TKGFLAWLLP VLIALPYMIW QRRLGELVRY 

       250        260        270        280        290        300 
GLVAVLVAIG ISLPWVLSIH AHEPDFWRFF FWHEHIRRFA ADNAQHTRPW WFYLPLLVAS 

       310        320        330        340        350        360 
SLPWAALLPG TFMQAWKDKR QAPTGFLLLW FLLPLAFFSL SRGKLPTYIM PCLLPLAVLM 

       370        380        390        400        410        420 
GSALIDRINA IQGRSIRINS LLNLLIGVAA MVALLYIQLT RPVYGHNEML GLSLVFIMLM 

       430        440        450        460        470        480 
GWIIANLLPA ARPLQYWPAP ALGIWLLVAL LPAGMPGFIV HNQMPDQFIK EHIEELRQTK 

       490        500        510        520        530        540 
TLLSNDLGAA SALAWRLQRP EVTLYNTEGE LKYGLAYADS AQRKVSMAEV GQWVSEARKQ 

       550        560        570        580 
GSVGVVMRVK DVVESEEVAL LPPGGKRYEE GNMLVLILPQ SQP

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000076 Genomic DNA. Translation: AAY93712.1.
RefSeqYP_261549.1. NC_004129.6.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING220664.PFL_4461.

Protein family/group databases

CAZyGT83. Glycosyltransferase Family 83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAY93712; AAY93712; PFL_4461.
GeneID3478580.
KEGGpfl:PFL_4461.
PATRIC19878354. VBIPseFlu72549_4566.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1807.
HOGENOMHOG000273002.
KOK07264.
OMAVVSPWGF.
OrthoDBEOG6NKQWN.
ProtClustDBPRK13279.

Enzyme and pathway databases

BioCycPFLU220664:GIX8-4496-MONOMER.
UniPathwayUPA00037.

Family and domain databases

HAMAPMF_01165. ArnT_transfer.
InterProIPR022839. ArnT_tfrase.
IPR003342. Glyco_trans_39.
[Graphical view]
PfamPF02366. PMT. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameARNT2_PSEF5
AccessionPrimary (citable) accession number: Q4K884
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: August 2, 2005
Last modified: February 19, 2014
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

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