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P99176 (KGUA_STAAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanylate kinase

EC=2.7.4.8
Alternative name(s):
GMP kinase
Gene names
Name:gmk
Ordered Locus Names:SA1052
OrganismStaphylococcus aureus (strain N315) [Complete proteome] [HAMAP]
Taxonomic identifier158879 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length207 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential for recycling GMP and indirectly, cGMP By similarity. HAMAP-Rule MF_00328

Catalytic activity

ATP + GMP = ADP + GDP. HAMAP-Rule MF_00328

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00328.

Sequence similarities

Belongs to the guanylate kinase family.

Contains 1 guanylate kinase-like domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpurine nucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

guanylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 207207Guanylate kinase HAMAP-Rule MF_00328
PRO_0000170605

Regions

Domain6 – 185180Guanylate kinase-like
Nucleotide binding13 – 208ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P99176 [UniParc].

Last modified October 11, 2004. Version 1.
Checksum: FE433434A722C98F

FASTA20724,022
        10         20         30         40         50         60 
MDNEKGLLIV LSGPSGVGKG TVRKRIFEDP STSYKYSISM TTRQMREGEV DGVDYFFKTR 

        70         80         90        100        110        120 
DAFEALIKDD QFIEYAEYVG NYYGTPVQYV KDTMDEGHDV FLEIEVEGAK QVRKKFPDAL 

       130        140        150        160        170        180 
FIFLAPPSLD HLRERLVGRG TESNEKIQSR INEARKEVEM MNLYDYVVVN DEVELAKNRI 

       190        200 
QCIVEAEHLK RERVEAKYRK MILEAKK 

« Hide

References

« Hide 'large scale' references
[1]"Whole genome sequencing of meticillin-resistant Staphylococcus aureus."
Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. expand/collapse author list , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K.
Lancet 357:1225-1240(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: N315.
[2]"Correlation of proteomic and transcriptomic profiles of Staphylococcus aureus during the post-exponential phase of growth."
Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y., Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C., Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.
J. Microbiol. Methods 60:247-257(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
Strain: N315.
[3]"Shotgun proteomic analysis of total and membrane protein extracts of S. aureus strain N315."
Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.
Submitted (OCT-2007) to UniProtKB
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Strain: N315.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000018 Genomic DNA. Translation: BAB42304.1.
PIRD89893.
RefSeqNP_374325.1. NC_002745.2.

3D structure databases

ProteinModelPortalP99176.
SMRP99176. Positions 5-197.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING158879.SA1052.

2D gel databases

SWISS-2DPAGEP99176.

Proteomic databases

PRIDEP99176.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB42304; BAB42304; BAB42304.
GeneID1123883.
KEGGsau:SA1052.
PATRIC19574324. VBIStaAur116463_1131.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000037639.
KOK00942.
OMAVELACDR.
OrthoDBEOG6CP410.

Enzyme and pathway databases

BioCycSAUR158879:GJCB-1112-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_00328. Guanylate_kinase.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR03263. guanyl_kin. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKGUA_STAAN
AccessionPrimary (citable) accession number: P99176
Secondary accession number(s): Q99UQ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: October 11, 2004
Last modified: May 14, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families