DNA gyrase subunit B - Streptococcus pyogenes serotype M18 (strain MGAS8232)

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Q8P1M4 (GYRB_STRP8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
DNA gyrase subunit B
EC=5.99.1.3

Gene names

Name:	gyrB
Ordered Locus Names:	spyM18_0795

Organism

Streptococcus pyogenes serotype M18 (strain MGAS8232) [Complete proteome] [HAMAP]

Taxonomic identifier

186103 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus ›

Protein attributes

Sequence length	650 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
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: 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 – 650

650

DNA gyrase subunit B HAMAP-Rule MF_01898

PRO_0000145352

Regions

Domain

429 – 543

115

Toprim

Sites

Metal binding

435

Magnesium 1; catalytic By similarity

Metal binding

508

Magnesium 1; catalytic By similarity

Metal binding

508

Magnesium 2 By similarity

Metal binding

510

Magnesium 2 By similarity

Site

460

Interaction with DNA By similarity

Site

463

Interaction with DNA By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q8P1M4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 2CF598897B872ACB
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FASTA

650

72,309

        10         20         30         40         50         60 
MIEENKHFEK KMQEYDASQI QVLEGLEAVR MRPGMYIGST AKEGLHHLVW EIVDNSIDEA 

        70         80         90        100        110        120 
LAGFASHIKV FIEADNSITV VDDGRGIPVD IQAKTGRPAV ETVFTVLHAG GKFGGGGYKV 

       130        140        150        160        170        180 
SGGLHGVGSS VVNALSTQLD VRVYKNGQIH YQEFKRGAVV ADLEIIGTTD VTGTTVHFTP 

       190        200        210        220        230        240 
DPEIFTETTQ FDYSVLAKRI QELAFLNRGL KISITDKRSG MEQEEHFHYE GGIGSYVEFL 

       250        260        270        280        290        300 
NDKKDVIFET PIYTDGELEG IAVEVAMQYT TSYQETVMSF ANNIHTHEGG THEQGFRAAL 

       310        320        330        340        350        360 
TRVINDYAKK NKILKENEDN LTGEDVREGL TAVISVKHPN PQFEGQTKTK LGNSEVVKIT 

       370        380        390        400        410        420 
NRLFSEAFQR FLLENPQVAR KIVEKGILAS KARIAAKRAR EVTRKKSGLE ISNLPGKLAD 

       430        440        450        460        470        480 
CSSNDANQNE LFIVEGDSAG GSAKSGRNRE FQAILPIRGK ILNVEKATMD KILANEEIRS 

       490        500        510        520        530        540 
LFTAMGTGFG ADFDVSKARY QKLVIMTDAD VDGAHIRTLL LTLIYRFMRP VLEAGYVYIA 

       550        560        570        580        590        600 
QPPIYGVKVG SEIKEYIQPG IDQEDQLKTA LEKYSIGRSK PTVQRYKGLG EMDDHQLWET 

       610        620        630        640        650 
TMDPENRLMA RVTVDDAAEA DKVFDMLMGD RVEPRRDFIE ENAVYSTLDI

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References

[1]

"Genome sequence and comparative microarray analysis of serotype M18 group A Streptococcus strains associated with acute rheumatic fever outbreaks."
Smoot J.C., Barbian K.D., Van Gompel J.J., Smoot L.M., Chaussee M.S., Sylva G.L., Sturdevant D.E., Ricklefs S.M., Porcella S.F., Parkins L.D., Beres S.B., Campbell D.S., Smith T.M., Zhang Q., Kapur V., Daly J.A., Veasy L.G., Musser J.M.
Proc. Natl. Acad. Sci. U.S.A. 99:4668-4673(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MGAS8232.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE009949 Genomic DNA. Translation: AAL97459.1.
RefSeq	NP_606960.1. NC_003485.1.
3D structure databases
ProteinModelPortal	Q8P1M4.
ModBase	Search...
Protein-protein interaction databases
STRING	186103.spyM18_0795.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAL97459; AAL97459; spyM18_0795.
GeneID	994970.
KEGG	spm:spyM18_0795.
PATRIC	19748210. VBIStrPyo4396_0695.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0187.
HOGENOM	HOG000075154.
KO	K02470.
OMA	IFETTEF.
ProtClustDB	PRK05644.
Family and domain databases
Gene3D	3.30.230.10. 1 hit. 3.30.565.10. 1 hit. 3.40.50.670. 1 hit.
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_STRP8

Accession

Primary (citable) accession number: Q8P1M4

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 30, 2005
Last sequence update:	October 1, 2002
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

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents