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Reviewed, UniProtKB/Swiss-Prot Q44270 (GYRB_ACIG3)

Last modified September 22, 2009. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    DNA gyrase subunit B
    EC=5.99.1.3
Gene names
Name: gyrB
OrganismAcinetobacter genomosp. 3
Taxonomic identifier48296 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length388 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

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.

Sequence similarities

Belongs to the type II topoisomerase family.

Ontologies

Keywords
   LigandATP-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

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA topoisomerase (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
PRO_0000145280

Experimental info

Non-terminal residue11
Non-terminal residue3881

Sequences

Sequence LengthMass (Da)Tools
Q44270-1 [UniParc].

Last modified January 11, 2001. Version 2.
Checksum: CD33473045902D59

FASTA38843,092
        10         20         30         40         50         60 
DNSYKVSGGL HGVGVSVVNA LSSKLHLIIN RAGQVHEQEY HHGDPQYPLR VIGETDSSGT 

        70         80         90        100        110        120 
TVRFWPSELT FSQTIFNVEI LARRLRELSF LNAGVRIVLR DERINLEHVY DYEGGLSEFV 

       130        140        150        160        170        180 
KYINEGKTHL NEIFHFTADT ENGIGVEVAL QWNESYQENV RCFTNNIPQK DGGTHLAGFR 

       190        200        210        220        230        240 
AALTRGLNQY LENENILKKE KVNVTGDDAR 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: 10028249] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 19004 / CIP 70.29.
[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: 8934907] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-118 AND 289-388.

Cross-references

Sequence databases

AB008686 Genomic DNA. Translation: BAA75403.1.
D73429 Genomic DNA. Translation: BAA11154.1.
D73414 Genomic DNA. Translation: BAA11139.1.

3D structure databases

HSSPHSSP built from PDB template 1EI1 based on UniProtKB P06982.
ModBaseSearch...

Family and domain databases

InterProIPR003594. ATP_bd_ATPase.
IPR014721. Ribosomal_S5_D2-typ_fold_subgr.
IPR001241. Topo_IIA_B/N.
IPR013506. Topo_IIA_B_2.
IPR018522. TopoIIA_CS.
[Graphical view]
Gene3DG3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit.
G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit.
PfamPF00204. DNA_gyraseB. 1 hit.
PF02518. HATPase_c. 1 hit.
[Graphical view]
PRINTSPR00418. TPI2FAMILY.
ProDomPD149633. DNA_gyrase_B. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00433. TOP2c. 1 hit.
[Graphical view]
PROSITEPS00177. TOPOISOMERASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGYRB_ACIG3
AccessionPrimary (citable) accession number: Q44270
Secondary accession number(s): Q60168, Q9ZA08
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 11, 2001
Last modified: September 22, 2009
This is version 42 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents