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B4EUL1 (ARNT1_PROMH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 38. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 1
EC=2.4.2.43
Alternative name(s):
4-amino-4-deoxy-L-arabinose lipid A transferase 1
Lipid IV(A) 4-amino-4-deoxy-L-arabinosyltransferase
Undecaprenyl phosphate-alpha-L-Ara4N transferase 1
Gene names
Name:arnT1
Ordered Locus Names:PMI0275
OrganismProteus mirabilis (strain HI4320) [Complete proteome] [HAMAP]
Taxonomic identifier529507 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Proteus ›

Protein attributes

Sequence length548 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 – 548548Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase 1 HAMAP-Rule MF_01165
PRO_0000380013

Regions

Transmembrane11 – 3121Helical; Potential
Transmembrane89 – 10921Helical; Potential
Transmembrane114 – 13421Helical; Potential
Transmembrane137 – 15721Helical; Potential
Transmembrane180 – 20021Helical; Potential
Transmembrane214 – 23421Helical; Potential
Transmembrane263 – 28321Helical; Potential
Transmembrane292 – 31221Helical; Potential
Transmembrane314 – 33421Helical; Potential
Transmembrane347 – 36721Helical; Potential
Transmembrane382 – 40221Helical; Potential
Transmembrane405 – 42521Helical; Potential

Sequences

Sequence LengthMass (Da)Tools
B4EUL1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: B7084221A0FD460C

FASTA54862,263
        10         20         30         40         50         60 
MNIAMTERYK WLLFFLFILL TYFIPLETRL LWQPDEIRYA EISREMLVSG NWSVPYLLDI 

        70         80         90        100        110        120 
RYFEKPVLGY WINCIAQWLF GESHFAVRIV VVTSTLLTGW LIYKAAMVVW RNSALAFNAM 

       130        140        150        160        170        180 
TVFLSSFLVL AIGTYNILDP IVTLFVTAAM YSFLVALSTP NKKGKIIAYM GIGFFCALGF 

       190        200        210        220        230        240 
LTKGFIAVVL PALVFLVMAI SQARFKEVVC YSSIALLALA ITAGPWVITV ALQAPDYWNY 

       250        260        270        280        290        300 
FFWVEHVQRF IAKESARSQP TWFYIPIVIL GVLPWLGFLF GALKSAFSLK KGTLYFLLWF 

       310        320        330        340        350        360 
TLFFAFFSAS KGKLLTYMLP CFVPLSILIA HYIEELKDRP DEKISKVNAS INIAFGLMGI 

       370        380        390        400        410        420 
SAVIYSLYSA KFALYDTNET LKIVLAISGF LFWSVIGAGA LFRQTQFLTM FCSIGLSLVI 

       430        440        450        460        470        480 
GYAIPEKIES RSTPENIIQR YYEPLSNKSY LLTDEVGIGT SLAWGLKRTD IRLTETKGEL 

       490        500        510        520        530        540 
AYGLNYPDVK NKYYSLEQLL ALIEANQYKG VAIVLVRPDR KQILTKLTTL KEKPIVEKEG 


DLTLVFFN

« Hide

References

[1]"Complete genome sequence of uropathogenic Proteus mirabilis, a master of both adherence and motility."
Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S., Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T., Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H., Rabbinowitsch E., Walker D., Whithead S. expand/collapse author list , Thomson N.R., Rather P.N., Parkhill J., Mobley H.L.T.
J. Bacteriol. 190:4027-4037(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HI4320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AM942759 Genomic DNA. Translation: CAR40745.1.
RefSeqYP_002150055.1. NC_010554.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING529507.PMI0275.

Protein family/group databases

CAZyGT83. Glycosyltransferase Family 83.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAR40745; CAR40745; PMI0275.
GeneID6802481.
KEGGpmr:PMI0275.
PATRIC20515209. VBIProMir120933_0265.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1807.
HOGENOMHOG000273002.
OMANIAMTER.
ProtClustDBPRK13279.

Enzyme and pathway databases

BioCycPMIR529507:GJIW-275-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 nameARNT1_PROMH
AccessionPrimary (citable) accession number: B4EUL1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: September 23, 2008
Last modified: May 1, 2013
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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