P0AG33 (RHO_SHIFL) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 65.
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: Transcription termination factor Rho EC=3.6.4.- Alternative name(s): ATP-dependent helicase Rho | ||||
| Gene names |
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| Organism | Shigella flexneri [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 623 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella![]() |
Protein attributes
| Sequence length | 419 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template By similarity. HAMAP-Rule MF_01884 |
| Subunit structure | Homohexamer. The homohexamer assembles into an open ring structure By similarity. |
| Sequence similarities | Belongs to the Rho family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Transcription Transcription regulation Transcription termination |
| Ligand | ATP-binding Nucleotide-binding RNA-binding |
| Molecular function | Helicase Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | DNA-dependent transcription, termination Inferred from electronic annotation. Source: HAMAP regulation of transcription, DNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP RNA bindingInferred from electronic annotation. Source: HAMAP RNA-dependent ATPase activityInferred from electronic annotation. Source: InterPro helicase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 419 | 419 | Transcription termination factor Rho HAMAP-Rule MF_01884 | PRO_0000188978 | |||||
Regions | |||||||||
| Nucleotide binding | 169 – 174 | 6 | ATP Potential | ||||||
| Nucleotide binding | 181 – 186 | 6 | ATP By similarity | ||||||
| Region | 61 – 66 | 6 | RNA-binding 1 By similarity | ||||||
| Region | 78 – 80 | 3 | RNA-binding 1 By similarity | ||||||
| Region | 108 – 110 | 3 | RNA-binding 1 By similarity | ||||||
| Region | 284 – 288 | 5 | RNA-binding 2 By similarity | ||||||
Sites | |||||||||
| Binding site | 212 | 1 | ATP By similarity | ||||||
| Site | 326 | 1 | RNA-binding 2 By similarity | ||||||
Sequences
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References
| [1] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE005674 Genomic DNA. Translation: AAN45293.2. AE014073 Genomic DNA. Translation: AAP18904.1. |
| RefSeq | NP_709586.2. NC_004337.2. NP_839093.1. NC_004741.1. |
3D structure databases | |
| ProteinModelPortal | P0AG33. |
| SMR | P0AG33. Positions 1-415. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 198214.SF3856. |
Proteomic databases | |
| PaxDb | P0AG33. |
| PRIDE | P0AG33. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAN45293; AAN45293; SF3856. AAP18904; AAP18904; S3903. |
| GeneID | 1025988. 1076538. |
| KEGG | sfl:SF3856. sfx:S3903. |
| PATRIC | 18709682. VBIShiFle31049_4256. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1158. |
| HOGENOM | HOG000076952. |
| KO | K03628. |
| ProtClustDB | PRK09376. |
Family and domain databases | |
| Gene3D | 2.40.50.140. 1 hit. |
| HAMAP | MF_01884. Rho. |
| InterPro | IPR003593. AAA+_ATPase. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR011129. Cold_shock_prot. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase. IPR011112. Rho_N. IPR011113. Rho_RNA-bd. IPR004665. Term_rho. [Graphical view] |
| Pfam | PF00006. ATP-synt_ab. 1 hit. PF07498. Rho_N. 1 hit. PF07497. Rho_RNA_bind. 1 hit. [Graphical view] |
| SMART | SM00382. AAA. 1 hit. SM00357. CSP. 1 hit. SM00959. Rho_N. 1 hit. [Graphical view] |
| SUPFAM | SSF50249. Nucleic_acid_OB. 1 hit. SSF68912. Rho_N. 1 hit. SSF52540. SSF52540. 1 hit. |
| TIGRFAMs | TIGR00767. rho. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RHO_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P0AG33 Secondary accession number(s): P03002, Q48357 | ||||||||
| 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
