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O07509

- PROJ_BACSU

UniProt

O07509 - PROJ_BACSU

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Protein

Glutamate 5-kinase 2

Gene

proJ

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.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131ATPUniRule annotation
Binding sitei53 – 531SubstrateUniRule annotation
Binding sitei140 – 1401SubstrateUniRule annotation
Binding sitei152 – 1521Substrate; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi172 – 1732ATPUniRule annotation
Nucleotide bindingi214 – 2207ATPUniRule annotation

GO - Molecular functioni

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

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 2UniRule annotation (EC:2.7.2.11UniRule annotation)
Alternative name(s):
Gamma-glutamyl kinase 2UniRule annotation
Short name:
GK 2UniRule annotation
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 UniRule annotation

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

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

Proteomic databases

PaxDbiO07509.

Interactioni

Protein-protein interaction databases

STRINGi224308.BSU18470.

Structurei

3D structure databases

ProteinModelPortaliO07509.
SMRiO07509. Positions 6-369.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 35677PUAUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the glutamate 5-kinase family.UniRule annotation
Contains 1 PUA domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0263.
HOGENOMiHOG000246369.
InParanoidiO07509.
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

        10         20         30         40         50
MTPDTSMKRV VVKIGSSSLT SLHGEISIRK LEALVDQVVK LKDAGYEVIL
60 70 80 90 100
VSSGAVAAGY RKLGFIQRPE KLPEKQASAS IGQGLLMEAY SKLFLAHGYV
110 120 130 140 150
ASQILITRSD FSDEYRYNNV RNTMNVLLER GIIPIINEND TVTVNRLKFG
160 170 180 190 200
DNDTLAAKVA GLIDADMLVI LSDIDGLYDG NPRTNPEAKK IQRVSEITPD
210 220 230 240 250
IEACAGDTGS IVGTGGMRSK LDAFKIVMAS GIKGFLGQAD AGDILYHAVH
260 270 280 290 300
EQAEGTYFEA EGTLPLNQKE QWIAFNSGPE GEMILSDDCS RKITNGQSSL
310 320 330 340 350
YLDGVQKIKG KFKSGSVVRL MDSKGTEIGL GIVNYSSVQL QEPEKKKELT
360 370
NRALIDQEAF VCHVDFSLPV N
Length:371
Mass (Da):40,354
Last modified:July 1, 1997 - v1
Checksum:i3352BFEFDECF703F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.
InParanoidi O07509.
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: October 29, 2014
This is version 105 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