Q52778 (NOLL_RHILO) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 60.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Nodulation protein NolL EC=2.3.1.- | ||||
| Gene names |
| ||||
| Organism | Rhizobium loti (strain MAFF303099) (Mesorhizobium loti) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 266835 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Phyllobacteriaceae › Mesorhizobium › ![]() |
Protein attributes
| Sequence length | 373 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred 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 process | Nodulation |
| Cellular component | Cell membrane Membrane |
| Domain | Transmembrane Transmembrane helix |
| Molecular function | Acyltransferase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | nodulation Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | transferase activity, transferring acyl groups other than amino-acyl groups Inferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 373 | 373 | Nodulation protein NolL | PRO_0000208082 | |||||
Regions | |||||||||
| Transmembrane | 27 – 47 | 21 | Helical; Potential | ||||||
| Transmembrane | 62 – 82 | 21 | Helical; Potential | ||||||
| Transmembrane | 98 – 118 | 21 | Helical; Potential | ||||||
| Transmembrane | 140 – 160 | 21 | Helical; Potential | ||||||
| Transmembrane | 164 – 184 | 21 | Helical; Potential | ||||||
| Transmembrane | 212 – 232 | 21 | Helical; Potential | ||||||
| Transmembrane | 253 – 273 | 21 | Helical; Potential | ||||||
| Transmembrane | 286 – 306 | 21 | Helical; Potential | ||||||
| Transmembrane | 324 – 344 | 21 | Helical; Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 4 | 1 | N → H in AAB50273. Ref.1 | ||||||
| Sequence conflict | 31 | 1 | G → A in AAB50273. Ref.1 | ||||||
| Sequence conflict | 121 | 1 | M → T in AAB50273. Ref.1 | ||||||
| Sequence conflict | 132 | 1 | S → L in AAB50273. Ref.1 | ||||||
| Sequence conflict | 163 | 1 | I → M in AAB50273. Ref.1 | ||||||
| Sequence conflict | 215 | 1 | W → S in AAB50273. Ref.1 | ||||||
| Sequence conflict | 221 | 1 | L → F in AAB50273. Ref.1 | ||||||
| Sequence conflict | 253 | 1 | Q → R in AAB50273. Ref.1 | ||||||
| Sequence conflict | 268 | 1 | A → R in AAB50273. Ref.1 | ||||||
| Sequence conflict | 326 | 1 | T → A in AAB50273. Ref.1 | ||||||
| Sequence conflict | 362 | 1 | R → H in AAB50273. Ref.1 | ||||||
| Sequence conflict | 365 | 1 | L → P in AAB50273. Ref.1 | ||||||
Sequences
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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. 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. |
| RefSeq | NP_106728.1. NC_002678.2. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 266835.mlr8757. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAB52514; BAB52514; BAB52514. |
| GeneID | 1229383. |
| KEGG | mlo:mlr8757. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG3594. |
| HOGENOM | HOG000113824. |
| KO | K00680. |
| OMA | FMAISGY. |
Enzyme and pathway databases | |
| BioCyc | MLOT266835:GJ9L-4876-MONOMER. |
Family and domain databases | |
| InterPro | IPR002656. Acyl_transf_3. [Graphical view] |
| Pfam | PF01757. Acyl_transf_3. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | NOLL_RHILO | ||||||||
| Accession | Primary (citable) accession number: Q52778 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
