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O07509

- PROJ_BACSU

UniProt

O07509 - PROJ_BACSU

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Protein
Glutamate 5-kinase 2
Gene
proJ, yohA, BSU18470
Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Catalyzes the transfer of a phosphate group to glutamate to form L-glutamate 5-phosphate By similarity.UniRule annotation

Catalytic activityi

ATP + L-glutamate = ADP + L-glutamate 5-phosphate.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131ATP By similarity
Binding sitei53 – 531Substrate By similarity
Binding sitei140 – 1401Substrate By similarity
Binding sitei152 – 1521Substrate; via amide nitrogen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1732ATP By similarity
Nucleotide bindingi214 – 2207ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. RNA binding Source: InterPro
  3. glutamate 5-kinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. L-proline biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Proline biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciBSUB:BSU18470-MONOMER.
UniPathwayiUPA00098; UER00359.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamate 5-kinase 2 (EC:2.7.2.11)
Alternative name(s):
Gamma-glutamyl kinase 2
Short name:
GK 2
Gene namesi
Name:proJ
Synonyms:yohA
Ordered Locus Names:BSU18470
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU18470. [Micado]

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 371371Glutamate 5-kinase 2UniRule annotation
PRO_0000109642Add
BLAST

Proteomic databases

PaxDbiO07509.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU18470.

Structurei

3D structure databases

ProteinModelPortaliO07509.
SMRiO07509. Positions 6-369.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 35677PUA
Add
BLAST

Sequence similaritiesi

Contains 1 PUA domain.

Phylogenomic databases

eggNOGiCOG0263.
HOGENOMiHOG000246369.
KOiK00931.
OMAiHGEISIR.
OrthoDBiEOG6PGK7G.
PhylomeDBiO07509.

Family and domain databases

Gene3Di2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPiMF_00456. ProB.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view]
PfamiPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFiPIRSF000729. GK. 1 hit.
PRINTSiPR00474. GLU5KINASE.
SMARTiSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMiSSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsiTIGR01027. proB. 1 hit.
PROSITEiPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O07509-1 [UniParc]FASTAAdd to Basket

« Hide

MTPDTSMKRV VVKIGSSSLT SLHGEISIRK LEALVDQVVK LKDAGYEVIL    50
VSSGAVAAGY RKLGFIQRPE KLPEKQASAS IGQGLLMEAY SKLFLAHGYV 100
ASQILITRSD FSDEYRYNNV RNTMNVLLER GIIPIINEND TVTVNRLKFG 150
DNDTLAAKVA GLIDADMLVI LSDIDGLYDG NPRTNPEAKK IQRVSEITPD 200
IEACAGDTGS IVGTGGMRSK LDAFKIVMAS GIKGFLGQAD AGDILYHAVH 250
EQAEGTYFEA EGTLPLNQKE QWIAFNSGPE GEMILSDDCS RKITNGQSSL 300
YLDGVQKIKG KFKSGSVVRL MDSKGTEIGL GIVNYSSVQL QEPEKKKELT 350
NRALIDQEAF VCHVDFSLPV N 371
Length:371
Mass (Da):40,354
Last modified:July 1, 1997 - v1
Checksum:i3352BFEFDECF703F
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006720 Genomic DNA. Translation: AAB62698.1.
AL009126 Genomic DNA. Translation: CAB13740.1.
PIRiF69682.
RefSeqiNP_389729.1. NC_000964.3.

Genome annotation databases

EnsemblBacteriaiCAB13740; CAB13740; BSU18470.
GeneIDi940098.
KEGGibsu:BSU18470.
PATRICi18975533. VBIBacSub10457_1957.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF006720 Genomic DNA. Translation: AAB62698.1 .
AL009126 Genomic DNA. Translation: CAB13740.1 .
PIRi F69682.
RefSeqi NP_389729.1. NC_000964.3.

3D structure databases

ProteinModelPortali O07509.
SMRi O07509. Positions 6-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU18470.

Proteomic databases

PaxDbi O07509.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB13740 ; CAB13740 ; BSU18470 .
GeneIDi 940098.
KEGGi bsu:BSU18470.
PATRICi 18975533. VBIBacSub10457_1957.

Organism-specific databases

GenoListi BSU18470. [Micado ]

Phylogenomic databases

eggNOGi COG0263.
HOGENOMi HOG000246369.
KOi K00931.
OMAi HGEISIR.
OrthoDBi EOG6PGK7G.
PhylomeDBi O07509.

Enzyme and pathway databases

UniPathwayi UPA00098 ; UER00359 .
BioCyci BSUB:BSU18470-MONOMER.

Family and domain databases

Gene3Di 2.30.130.10. 1 hit.
3.40.1160.10. 1 hit.
HAMAPi MF_00456. ProB.
InterProi IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
IPR002478. PUA.
IPR015947. PUA-like_domain.
[Graphical view ]
Pfami PF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view ]
PIRSFi PIRSF000729. GK. 1 hit.
PRINTSi PR00474. GLU5KINASE.
SMARTi SM00359. PUA. 1 hit.
[Graphical view ]
SUPFAMi SSF53633. SSF53633. 1 hit.
SSF88697. SSF88697. 1 hit.
TIGRFAMsi TIGR01027. proB. 1 hit.
PROSITEi PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The salt-inducible proHJ operon involved in proline biosynthesis in Bacillus subtilis."
    Belitsky B.R., Sonenshein A.L.
    Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 168 / SMY.
  2. "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
    Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V.
    , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
    Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 168.

Entry informationi

Entry nameiPROJ_BACSU
AccessioniPrimary (citable) accession number: O07509
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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