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Q5HTT7 (KGUA_CAMJR) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 54. 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:CJE1311
OrganismCampylobacter jejuni (strain RM1221) [Complete proteome] [HAMAP]
Taxonomic identifier195099 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length205 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 – 205205Guanylate kinase HAMAP-Rule MF_00328
PRO_0000266300

Regions

Domain3 – 183181Guanylate kinase-like
Nucleotide binding10 – 178ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5HTT7 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: D9F5221A7B073A2F

FASTA20523,784
        10         20         30         40         50         60 
MQGFVLLISG PSGAGKSTLL KKLFDEFEDE LYFSISSTTR KPREGEKNGI HYHFISHEEF 

        70         80         90        100        110        120 
QKGIDSDHFL EWARVHENFY GTSLKHTQNA LDNGKIVVFD IDVQGFKIAR KKMADKIVSV 

       130        140        150        160        170        180 
FITTKNKDEL KKRLIKRNTD TIIQLEKRLQ NASDEMKELS EYDYLIINDE LKQSYEALRA 

       190        200 
ILIAHKFRTK GQNLGQIQNI WNEGE 

« Hide

References

[1]"Major structural differences and novel potential virulence mechanisms from the genomes of multiple Campylobacter species."
Fouts D.E., Mongodin E.F., Mandrell R.E., Miller W.G., Rasko D.A., Ravel J., Brinkac L.M., DeBoy R.T., Parker C.T., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R., Sullivan S.A., Shetty J.U., Ayodeji M.A., Shvartsbeyn A., Schatz M.C. expand/collapse author list , Badger J.H., Fraser C.M., Nelson K.E.
PLoS Biol. 3:72-85(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RM1221.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000025 Genomic DNA. Translation: AAW35632.1.
RefSeqYP_179298.1. NC_003912.7.

3D structure databases

ProteinModelPortalQ5HTT7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING195099.CJE1311.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW35632; AAW35632; CJE1311.
GeneID3231818.
KEGGcjr:CJE1311.
PATRIC20044422. VBICamJej134361_1329.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000037638.
KOK00942.
OMARCILDIE.
OrthoDBEOG6CP410.
ProtClustDBPRK00300.

Enzyme and pathway databases

BioCycCJEJ195099:GJC0-1337-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_CAMJR
AccessionPrimary (citable) accession number: Q5HTT7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: February 15, 2005
Last modified: April 16, 2014
This is version 54 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