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Q52778 (NOLL_RHILO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
Nodulation protein NolL

EC=2.3.1.-
Gene names
Name:nolL
Ordered Locus Names:mlr8757
OrganismRhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP]
Taxonomic identifier266835 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesPhyllobacteriaceaeMesorhizobium

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Thought to be an acetyltransferase that modifies the fucose of the nod factor.

Subcellular location

Cell membrane; Multi-pass membrane protein Potential.

Sequence similarities

Belongs to the acyltransferase 3 family.

Ontologies

Keywords
   Biological processNodulation
   Cellular componentCell membrane
Membrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processnodulation

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiontransferase activity, transferring acyl groups other than amino-acyl groups

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 373373Nodulation protein NolL
PRO_0000208082

Regions

Transmembrane27 – 4721Helical; Potential
Transmembrane62 – 8221Helical; Potential
Transmembrane98 – 11821Helical; Potential
Transmembrane140 – 16021Helical; Potential
Transmembrane164 – 18421Helical; Potential
Transmembrane212 – 23221Helical; Potential
Transmembrane253 – 27321Helical; Potential
Transmembrane286 – 30621Helical; Potential
Transmembrane324 – 34421Helical; Potential

Experimental info

Sequence conflict41N → H in AAB50273. Ref.1
Sequence conflict311G → A in AAB50273. Ref.1
Sequence conflict1211M → T in AAB50273. Ref.1
Sequence conflict1321S → L in AAB50273. Ref.1
Sequence conflict1631I → M in AAB50273. Ref.1
Sequence conflict2151W → S in AAB50273. Ref.1
Sequence conflict2211L → F in AAB50273. Ref.1
Sequence conflict2531Q → R in AAB50273. Ref.1
Sequence conflict2681A → R in AAB50273. Ref.1
Sequence conflict3261T → A in AAB50273. Ref.1
Sequence conflict3621R → H in AAB50273. Ref.1
Sequence conflict3651L → P in AAB50273. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q52778 [UniParc].

Last modified June 1, 2001. Version 2.
Checksum: 24D21ED82AA232AF

FASTA37341,866
        10         20         30         40         50         60 
MLDNIRAGAK GRGSCPAGTN NRDLSFDFAK GILITLVIIG HLLQYLIYQG TDAFWLSPYF 

        70         80         90        100        110        120 
KSIYMFHMPL FMAISGYLSS GAILRKSFTQ GVGERAMQLL LPMLFWCTLI WTLKSAVIFP 

       130        140        150        160        170        180 
MKSLTDTLLD LSTEVIGTYW FIWAAFISFI LIRVLTTFNR LSIWIISASA IAVAFAPITL 

       190        200        210        220        230        240 
SITPLLKYTY PFYCLGFLFA QPIGWQNGVI WRYKWIFVVL LSIAAFICFL GWGKETYAYN 

       250        260        270        280        290        300 
NLVLIHDEQS AKQVFLMFSG SLAASAVAMQ SMFQCWRLVY STRVARFVAV QLGQSTLLLY 

       310        320        330        340        350        360 
LVQGAVFRLM DLIQFGEVWN LTTRITFATV LGVAIVVIAM AIRSIARNLG YVSRIVVGAP 

       370 
PRPSLLKSQS VIN 

« Hide

References

« Hide 'large scale' references
[1]"Novel and complex chromosomal arrangement of Rhizobium loti nodulation genes."
Scott D.B., Young C.A., Collins-Emerson J.M., Terzaghi E.A., Rockman E.S., Lewis P.E., Pankhurst C.E.
Mol. Plant Microbe Interact. 9:187-197(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: NZP 2213.
[2]"Complete genome structure of the nitrogen-fixing symbiotic bacterium Mesorhizobium loti."
Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S., Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y., Nakayama S. expand/collapse author list , Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M., Tabata S.
DNA Res. 7:331-338(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MAFF303099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U22899 Genomic DNA. Translation: AAB50273.1.
BA000012 Genomic DNA. Translation: BAB52514.1.
RefSeqNP_106728.1. NC_002678.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING266835.mlr8757.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB52514; BAB52514; BAB52514.
GeneID1229383.
KEGGmlo:mlr8757.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG3594.
HOGENOMHOG000113824.
OMAFMAISGY.
OrthoDBEOG6FRD2N.

Enzyme and pathway databases

BioCycMLOT266835:GJ9L-4876-MONOMER.

Family and domain databases

InterProIPR002656. Acyl_transf_3.
[Graphical view]
PfamPF01757. Acyl_transf_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameNOLL_RHILO
AccessionPrimary (citable) accession number: Q52778
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 63 of the entry and version 2 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