P22118 (GYRB_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA gyrase subunit B
EC=5.99.1.3

Gene names

Name:

gyrB

Organism

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	781 AA.
Sequence status	Complete.
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 By similarity. HAMAP-Rule MF_01898
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA. HAMAP-Rule MF_01898
Cofactor	Magnesium. Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ and Ca2+ By similarity.
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 component	Cytoplasm
Ligand	ATP-binding DNA-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Isomerase Topoisomerase
Gene Ontology (GO)
Biological_process	DNA topological change Inferred from electronic annotation. Source: InterPro DNA-dependent DNA replication Inferred from electronic annotation. Source: HAMAP
Cellular_component	chromosome Inferred from electronic annotation. Source: InterPro cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP DNA topoisomerase type II (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 781	781	DNA gyrase subunit B HAMAP-Rule MF_01898		PRO_0000145327
Regions
	Domain	421 – 522	102	Toprim
Sites
	Metal binding	427	1	Magnesium 1; catalytic By similarity
	Metal binding	487	1	Magnesium 1; catalytic By similarity
	Metal binding	487	1	Magnesium 2 By similarity
	Metal binding	489	1	Magnesium 2 By similarity
	Site	452	1	Interaction with DNA By similarity
	Site	455	1	Interaction with DNA By similarity

Sequences

	Sequence		Length	Mass (Da)
	P22118 [UniParc]. Last modified August 1, 1991. Version 1. Checksum: 8F9F6AE69F8B25BE	FASTA	781	86,516
	10 20 30 40 50 60 MTEQKHEEYG ADSIQVLEGL EAVPKRPGMY IGDTQDGSGL HHMVFEVLDN AIDEALAGHC 70 80 90 100 110 120 DKITVTIHAD HSVSVADNGR GMPTGIHPKE GRSAAEVIMT VLHAGGKFDN NSYKISGGLH 130 140 150 160 170 180 GVGVSVVNAL SDWVTLTIYR DGKEHFVRFV RGETEEPLKI VGDSDKKGTT VRFLAGTETF 190 200 210 220 230 240 GNIEYSFDIL AKRIRELSFL NNGVDIELTD ERDGKHESFA LSGGVAGFVQ YMNRKKTPLH 250 260 270 280 290 300 EKIFYAFGEK DGMSVECAMQ WNDSYQESVQ CFTNNIPQRD GGTHLTALRQ VMTRTINSYI 310 320 330 340 350 360 EANEVAKKAK VETAGDDMRE GLTCVLSVKL PDPKFSSQTK DKLVSGEIGP VVNEVINQAL 370 380 390 400 410 420 TDFLEENPNE AKIITGKIVD AARARQAARK AREITRRKGL MDGLGLPGKL ADCQEKDPAL 430 440 450 460 470 480 SELYLVEGNS AGGSAMQGRD RKFQAILPLK GKILNVATLI TALGAGIGKE EFNPEKLRYH 490 500 510 520 530 540 RIIIMTDADV DGAHIRTLLL TFFYRQMPDL VERGYIYIAQ PPLYKAKYGK QERYLKDELE 550 560 570 580 590 600 KDQWLLGLAL EKAKIVSDGR TIEGAELADT AKQFLLAKTV IEQESRFVDE LVLRAMLHAS 610 620 630 640 650 660 PIDLTSSENA DKAVAELSGL LDEKEAALER IEGHEGHQFI KITRKLHGNV MVSYIEPKFL 670 680 690 700 710 720 NSKAYQTLTQ TAAALKGLVG EGAKLYKGEN EYDADSFETA LDILMSVAQK GMSIQRYKGL 730 740 750 760 770 780 GEMNPEQLWE TTMDPTVRRL LKVRIEDRIA DEVFVTLMGD EVEPRRAFIE NNALIAQNID A

References

[1]

"Characterization of a gyrB mutation responsible for low-level nalidixic acid resistance in Neisseria gonorrhoeae." Stein D.C., Danaher R.J., Cook T.M. Antimicrob. Agents Chemother. 35:622-626(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: WR302 / MUG116.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M59981 Genomic DNA. Translation: AAA88327.1.
PIR	A49794.
3D structure databases
ProteinModelPortal	P22118.
SMR	P22118. Positions 14-380.
ModBase	Search...
Proteomic databases
PRIDE	P22118.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.30.230.10. 1 hit. 3.30.565.10. 1 hit. 3.40.50.670. 2 hits.
HAMAP	MF_01898. GyrB.
InterPro	IPR002288. DNA_gyrase_B_C. IPR011557. GyrB. IPR003594. 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]
Pfam	PF00204. DNA_gyraseB. 1 hit. PF00986. DNA_gyraseB_C. 1 hit. PF02518. HATPase_c. 1 hit. PF01751. Toprim. 1 hit. [Graphical view]
PRINTS	PR00418. TPI2FAMILY.
SMART	SM00387. HATPase_c. 1 hit. SM00433. TOP2c. 1 hit. [Graphical view]
SUPFAM	SSF55874. ATP_bd_ATPase. 1 hit. SSF54211. Ribosomal_S5_D2-typ_fold. 1 hit. SSF56719. Topo_IIA_cen. 1 hit.
TIGRFAMs	TIGR01059. gyrB. 1 hit.
PROSITE	PS00177. TOPOISOMERASE_II. 1 hit. PS50880. TOPRIM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GYRB_NEIGO

Accession

Primary (citable) accession number: P22118

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program