Q0BVD3 (Q0BVD3_GRABC) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Recommended name:
DNA gyrase subunit B HAMAP MF_01898
EC=5.99.1.3 HAMAP MF_01898

Gene names

Name:	gyrB HAMAP MF_01898
Ordered Locus Names:	GbCGDNIH1_0321

Organism

Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1) [Complete proteome] [HAMAP] EMBL ABI61219.1

Taxonomic identifier

391165 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodospirillales › Acetobacteraceae › Granulibacter

Protein attributes

Sequence length	810 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 MF_01898
Catalytic activity	ATP-dependent breakage, passage and rejoining of double-stranded DNA. SAAS SAAS002288 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 By similarity. HAMAP MF_01898
Subcellular location	Cytoplasm By similarity HAMAP MF_01898.
Sequence similarities	Belongs to the type II topoisomerase family. HAMAP MF_01898 Contains 1 Toprim domain. SAAS SAAS002288 HAMAP MF_01898

Ontologies

Keywords
Cellular component	Cytoplasm HAMAP MF_01898
Ligand	ATP-binding SAAS SAAS002288 HAMAP MF_01898 Nucleotide-binding
Molecular function	Isomerase Topoisomerase SAAS SAAS002288 HAMAP MF_01898
Technical term	Complete proteome
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: HAMAP
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP DNA topoisomerase (ATP-hydrolyzing) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q0BVD3 [UniParc]. Last modified October 17, 2006. Version 1. Checksum: 4FC5F853D726681C	FASTA	810	88,488
	10 20 30 40 50 60 MSDPTPLPPD SDAYDASSIS VLRGLDAVRK RPGMYIGDTD DGSGLHHMAF EIIDNAVDEA 70 80 90 100 110 120 QAGFASEVTL TLNGDGSVTV TDDGRGIPTD IHAEEGISAA EVVLTRLHAG GKFNQNSYKV 130 140 150 160 170 180 SGGLHGVGAA VVNALSEWME VRIWREGREH FIRFRHGDAE APLVEIGPSP RGSGTQVTFK 190 200 210 220 230 240 PSNLTFTRVE FEFATLERRL RELAFLNSGL KIVLRDERHV PAQESVFCYE GGLTAFVEWL 250 260 270 280 290 300 DRGKVALFDP PISAAGSANA DQGDIKVEFS LVWNDSFHET MLCFTNNIPQ RDGGTHLAGF 310 320 330 340 350 360 RQALTRVVSK YAEGLGKKEQ LALVGEDMRE GMTAVLSVKV PDPKFSSQTK EKLVSSEVQP 370 380 390 400 410 420 VVHAAVADAI GHWFETHPKE TRSIIQKAMD AASAREAARR ARELTRRKGV LDISSLPGKL 430 440 450 460 470 480 ADCQERDPSK CEIFIVEGDS AGGSAKQGRD RKFQAILPLK GKILNVERAR FDRMLGSAEI 490 500 510 520 530 540 GTLITALGTG IGRGEPEQGG FDIAKLRYHR IVIMTDADVD GSHIRTLLLT FFFRQMPQLF 550 560 570 580 590 600 TNGHLYIAQP PLFKATRGKD ERYLKDERAL EEYLLSKALN EAQLTLADGR VFAGDELAEE 610 620 630 640 650 660 VNHLRDVAAR MRRLAGGIPL ALLEQAVVAG ALRPDATPDT LQTLSARLNA ISPASERGWI 670 680 690 700 710 720 VASEGEGLTM RRTVRGVAER HTLEATALRS AEARWLAERT DQLAARYTQP VSLALDAARL 730 740 750 760 770 780 ELAGPASVLE RILAHGRKGL SFQRFKGLGE MNPEQLWSTT LDPATRTLLQ VKVGDIEDAG 790 800 810 QIFSTLMGDV VEPRRDFIVG NALKVANLDV

References

[1]

"Genome sequence analysis of the emerging human pathogenic acetic acid bacterium Granulibacter bethesdensis." Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E., Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M. J. Bacteriol. 189:8727-8736(2007) [PubMed: 17827295] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000394 Genomic DNA. Translation: ABI61219.1.
RefSeq	YP_744142.1. NC_008343.1.
3D structure databases
ProteinModelPortal	Q0BVD3.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0BVD3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4276361.
GenomeReviews	Gene locus GbCGDNIH1_0321 in contig CP000394_GR.
KEGG	gbe:GbCGDNIH1_0321.
NMPDR	fig|391165.8.peg.326.
PATRIC	22076687. VBIGraBet83793_0339.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0187.
HOGENOM	HBG304889.
OMA	DCSSRDP.
PhylomeDB	Q0BVD3.
ProtClustDB	PRK14939.
Family and domain databases
HAMAP	MF_01898. GyrB. [Tree]
InterPro	IPR003594. ATPase-like_ATP-bd. IPR011557. GyrB. IPR020568. Ribosomal_S5_D2-typ_fold. IPR014721. Ribosomal_S5_D2-typ_fold_subgr. IPR001241. Topo_IIA. IPR013759. Topo_IIA_B/N_ab. IPR002288. Topo_IIA_B_C. IPR013506. Topo_IIA_bsu_dom2. IPR013760. Topo_IIA_cen. IPR018522. TopoIIA_CS. IPR006171. Toprim_domain. [Graphical view]
Gene3D	G3DSA:3.30.565.10. ATP_bd_ATPase. 1 hit. G3DSA:3.30.230.10. Ribosomal_S5_D2-type_fold. 1 hit. G3DSA:3.40.50.670. Topo_IIA_B/N_ab. 2 hits.
KO	K02470.
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. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

Q0BVD3_GRABC

Accession

Primary (citable) accession number: Q0BVD3

Entry history

Integrated into UniProtKB/TrEMBL:	October 17, 2006
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)