Q44277 (GYRB_ACIS6) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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: DNA gyrase subunit B EC=5.99.1.3 | ||
| Gene names |
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| Organism | Acinetobacter sp. (strain ATCC 31012) | ||
| Taxonomic identifier | 68991 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Moraxellaceae › Acinetobacter |
Protein attributes
| Sequence length | 216 AA. |
| Sequence status | Fragments. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | DNA gyrase negatively supercoils closed circular double-stranded DNA in an ATP-dependent manner and also catalyzes the interconversion of other topological isomers of double-stranded DNA rings, including catenanes and knotted rings. HAMAP MF_01898 |
| Catalytic activity | ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP MF_01898 |
| Subunit structure | Made up of two chains. The A chain is responsible for DNA breakage and rejoining; the B chain catalyzes ATP hydrolysis. The enzyme forms an A2B2 tetramer. |
| Subcellular location | Cytoplasm Potential HAMAP MF_01898. |
| Sequence similarities | Belongs to the type II topoisomerase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Isomerase Topoisomerase |
| Gene Ontology (GO) | |
| Biological process | DNA topological change Inferred from electronic annotation. Source: InterPro |
| Cellular component | chromosome Inferred from electronic annotation. Source: InterPro cytoplasmInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA topoisomerase (ATP-hydrolyzing) activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | ‹1 – ›216 | ›216 | DNA gyrase subunit B HAMAP MF_01898 | PRO_0000145285 | |||||
Experimental info | |||||||||
| Non-adjacent residues | 116 – 117 | 2 | |||||||
| Non-terminal residue | 1 | 1 | |||||||
| Non-terminal residue | 216 | 1 | |||||||
Sequences
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References
| [1] | "Phylogenetic analysis of Acinetobacter strains based on the nucleotide sequences of gyrB genes and on the amino acid sequences of their products." Yamamoto S., Harayama S. Int. J. Syst. Bacteriol. 46:506-511(1996) [PubMed: 8934907] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D73440 Genomic DNA. Translation: BAA11165.1. D73425 Genomic DNA. Translation: BAA11150.1. |
3D structure databases | |
| ProteinModelPortal | Q44277. |
| SMR | Q44277. Positions 1-114. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| HAMAP | MF_01898. GyrB. [Tree] |
| InterPro | IPR003594. ATPase-like_ATP-bd. IPR001241. Topo_IIA. IPR013759. Topo_IIA_B/N_ab. IPR013760. Topo_IIA_cen. IPR018522. TopoIIA_CS. [Graphical view] |
| Gene3D | G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. G3DSA:3.40.50.670. Topo_IIA_B/N_ab. 1 hit. |
| SMART | SM00433. TOP2c. 1 hit. [Graphical view] |
| SUPFAM | SSF55874. ATP_bd_ATPase. 1 hit. SSF56719. Topo_IIA_cen. 1 hit. |
| PROSITE | PS00177. TOPOISOMERASE_II. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GYRB_ACIS6 | ||||||||
| Accession | Primary (citable) accession number: Q44277 Secondary accession number(s): Q60168 | ||||||||
| 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 |

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