gyrB protein (Klebsiella pneumoniae) - STRING interaction network
"gyrB" - DNA gyrase subunit B in Klebsiella pneumoniae
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
Your Input:
Gene Fusion
gyrBDNA gyrase subunit B; Negatively supercoils closed circular double-stranded DNA; Derived by automated computational analysis using gene prediction method- Protein Homology (804 aa)    
Predicted Functional Partners:
DNA gyrase subunit A; A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner (877 aa)
DNA topoisomerase 4 subunit A; Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule; Belongs to the type II topoisomerase GyrA/ParC subunit family. ParC type 1 subfamily (752 aa)
DNA replication and repair protein RecF; The RecF protein is involved in DNA metabolism; it is required for DNA replication and normal SOS inducibility. RecF binds preferentially to single-stranded, linear DNA. It also seems to bind ATP (357 aa)
Chromosomal replication initiator protein DnaA; Plays an important role in the initiation and regulation of chromosomal replication. Binds to the origin of replication; it binds specifically double-stranded DNA at a 9 bp consensus (dnaA box)- 5’-TTATC[CA]A[CA]A-3’. DnaA binds to ATP and to acidic phospholipids (467 aa)
DNA polymerase III beta subunit; Binds the polymerase to DNA and acts as a sliding clamp; Derived by automated computational analysis using gene prediction method- Protein Homology (366 aa)
DNA gyrase inhibitor YacG; Inhibits all the catalytic activities of DNA gyrase by preventing its interaction with DNA. Acts by binding directly to the C-terminal domain of GyrB, which probably disrupts DNA binding by the gyrase (64 aa)
RNA polymerase sigma factor RpoD; Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is the primary sigma factor during exponential growth (613 aa)
Protein RecA; Can catalyze the hydrolysis of ATP in the presence of single-stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex DNA, and the ATP-dependent hybridization of homologous single-stranded DNAs. It interacts with LexA causing its activation and leading to its autocatalytic cleavage (352 aa)
Leucyl-tRNA synthetase; leucine--tRNA ligase; LeuRS; class-I aminoacyl-tRNA synthetase; charges leucine by linking carboxyl group to alpha-phosphate of ATP and then transfers aminoacyl-adenylate to its tRNA; due to the large number of codons that tRNA(Leu) recognizes, the leucyl-tRNA synthetase does not recognize the anticodon loop of the tRNA, but instead recognition is dependent on a conserved discriminator base A37 and a long arm; an editing domain hydrolyzes misformed products; in Methanothermobacter thermautotrophicus this enzyme associates with prolyl-tRNA synthetase; Derived by [...] (860 aa)
DNA-directed RNA polymerase subunit beta; DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates; beta subunit is part of the catalytic core which binds with a sigma factor to produce the holoenzyme; Derived by automated computational analysis using gene prediction method- Protein Homology (1342 aa)
Your Current Organism:
Klebsiella pneumoniae
NCBI taxonomy Id: 573
Other names: ATCC 13883, Bacillus pneumoniae, Bacterium pneumoniae crouposae, CCUG 225, CIP 82.91, DSM 30104, HAMBI 450, Hyalococcus pneumoniae, IFO 14940, K. pneumoniae, Klebsiella pneumoniae, Klebsiella sp. M-AI-2, Klebsiella sp. PB12, Klebsiella sp. RCE-7, LMG 2095, NBRC 14940, NCTC 9633
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