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Q44065 (GYRB_ACIHA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 67. 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:
DNA gyrase subunit B

EC=5.99.1.3
Gene names
Name:gyrB
OrganismAcinetobacter haemolyticus
Taxonomic identifier29430 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length388 AA.
Sequence statusFragment.
Protein existenceInferred 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 By similarity. HAMAP-Rule MF_01898

Catalytic activity

ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP-Rule MF_01898

Subunit structure

Heterotetramer, composed of two GyrA and two GyrB chains. Within the heterotetramer, GyrA contains the active site tyrosine that forms a covalent intermediate with the DNA, while GyrB contributes the cofactor binding sites and catalyzes ATP hydrolysis By similarity.

Subcellular location

Cytoplasm Potential HAMAP-Rule MF_01898.

Sequence similarities

Belongs to the type II topoisomerase family.

Contains 1 Toprim domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionIsomerase
Topoisomerase
Gene Ontology (GO)
   Biological_processDNA topological change

Inferred from electronic annotation. Source: InterPro

   Cellular_componentchromosome

Inferred from electronic annotation. Source: InterPro

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase type II (ATP-hydrolyzing) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›388›388DNA gyrase subunit B HAMAP-Rule MF_01898
PRO_0000145276

Regions

Domain312 – ›388›77Toprim

Sites

Site3431Interaction with DNA By similarity
Site3461Interaction with DNA By similarity

Experimental info

Sequence conflict121G → R in BAA11155. Ref.2
Non-terminal residue11
Non-terminal residue3881

Sequences

Sequence LengthMass (Da)Tools
Q44065 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: 076699E07CE72FBA

FASTA38843,103
        10         20         30         40         50         60 
DNSYKVSGGL HGVGVSVVNA LSSKLQLTIH RAGQEHQQEY HHGDPQYPLR VIGETDRTGT 

        70         80         90        100        110        120 
IVRFWPSAET FSQTIFNVDI LARRLRELSF LNAGVRIVLR DERVNLENVY DYEGGLSEFV 

       130        140        150        160        170        180 
RYINEGKTHL NEIFHFTTDA DNGISVEVAL QWNDSYQENV RCFTNNIPQK DGGTHLAGFR 

       190        200        210        220        230        240 
AALTRGLNSY MENENLLKKE KVVVSGDDAR EGLTAIISVK VPDPKFSSQT KEKLVSSEVK 

       250        260        270        280        290        300 
PAVEQAMNKE FSAYLLENPQ AAKSIAGKII DAARARDAAR KAREMTRRKS ALDIAGLPGK 

       310        320        330        340        350        360 
LADCQEKDPA LSELYLVEGD SAGGSAKQGR NRKMQAILPL KGKILNVERA RFDKMISSQE 

       370        380 
VGTLITALGC GIGREEYNPD KLRYHKII 

« Hide

References

[1]"Phylogenetic structures of the genus Acinetobacter based on gyrB sequences: comparison with the grouping by DNA-DNA hybridization."
Yamamoto S., Bouvet P.J.M., Harayama S.
Int. J. Syst. Bacteriol. 49:87-95(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 17906 / NCTC 10305 / CIP 64.3 / B40 and ATCC 17907 / CIP 64.4 / B44.
[2]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-118 AND 289-388.
Strain: ATCC 17906 / NCTC 10305 / CIP 64.3 / B40.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB008691 Genomic DNA. Translation: BAA75408.1.
AB008724 Genomic DNA. Translation: BAA75441.1.
D73430 Genomic DNA. Translation: BAA11155.1.
D73415 Genomic DNA. Translation: BAA11140.1.
PIRT43904.

3D structure databases

ProteinModelPortalQ44065.
SMRQ44065. Positions 1-286.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.30.230.10. 1 hit.
3.30.565.10. 1 hit.
3.40.50.670. 1 hit.
HAMAPMF_01898. GyrB.
InterProIPR003594. HATPase_ATP-bd.
IPR020568. Ribosomal_S5_D2-typ_fold.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR001241. Topo_IIA.
IPR013506. Topo_IIA_bsu_dom2.
IPR013759. Topo_IIA_cen_dom.
IPR013760. Topo_IIA_like_dom.
IPR018522. TopoIIA_CS.
IPR006171. Toprim_domain.
[Graphical view]
PfamPF00204. DNA_gyraseB. 1 hit.
PF01751. Toprim. 1 hit.
[Graphical view]
PRINTSPR00418. TPI2FAMILY.
SMARTSM00433. TOP2c. 1 hit.
[Graphical view]
SUPFAMSSF55874. ATP_bd_ATPase. 1 hit.
SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit.
SSF56719. Topo_IIA_cen. 1 hit.
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
PS50880. TOPRIM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGYRB_ACIHA
AccessionPrimary (citable) accession number: Q44065
Secondary accession number(s): Q59120, Q9ZA03
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: May 1, 2013
This is version 67 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