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P39820 (PROB_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamate 5-kinase 1
EC=2.7.2.11
Alternative name(s):
Gamma-glutamyl kinase 1
Short name=GK 1
Gene names
Name:proB
Ordered Locus Names:BSU13120
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length365 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of a phosphate group to glutamate to form glutamate 5-phosphate which rapidly cyclizes to 5-oxoproline. HAMAP-Rule MF_00456

Catalytic activity

ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP-Rule MF_00456

Pathway

Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP-Rule MF_00456

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the glutamate 5-kinase family.

Contains 1 PUA domain.

Ontologies

Keywords
   Biological processAmino-acid biosynthesis
Proline biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processL-proline biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: InterPro

glutamate 5-kinase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 365365Glutamate 5-kinase 1 HAMAP-Rule MF_00456
PRO_0000109641

Regions

Domain276 – 35378PUA
Nucleotide binding168 – 1692ATP By similarity
Nucleotide binding210 – 2167ATP By similarity

Sites

Binding site91ATP By similarity
Binding site491Substrate By similarity
Binding site1361Substrate By similarity
Binding site1481Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict25 – 328AKIREHVQ → QNQRACS in BAA05044. Ref.1
Sequence conflict511A → P in CAA05591. Ref.2
Sequence conflict541A → R in CAA05591. Ref.2
Sequence conflict181 – 1855NPEAK → ILSE in BAA05044. Ref.1
Sequence conflict357 – 3659Missing in BAA05044. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P39820 [UniParc].

Last modified June 16, 2009. Version 3.
Checksum: D5B8DB471ADE62E2

FASTA36539,346
        10         20         30         40         50         60 
MKKQRIVVKI GSSSLTNSKG SIDEAKIREH VQAISVLKKA GHEMILITSG AVAAGFSSLG 

        70         80         90        100        110        120 
YPSRPVTIKG KQAAAAVGQT LLMQQYMNQF KQYSLTPGQI LLTRNDFSKR ERYRNAYATI 

       130        140        150        160        170        180 
MELLERGVIP IINENDSTSV EELTFGDNDM LSALVSGLIH ADQLMILTDI NGLYDANPNE 

       190        200        210        220        230        240 
NPEAKRFDYL PEITPELLGY AGSAGSKVGT GGMKSKLLAT QTALSLGVKV FIGTGSGEQK 

       250        260        270        280        290        300 
LADILDGRGD GTYIGDKELS SVNNTRQWIQ FHSPISGEII IDAGAEEAMI HNGSSLLPAG 

       310        320        330        340        350        360 
VVGVNGSFPK GAVVEVRGPG GVIGKGQTHY SSEEIMEAKG KRSDELDFEK TFEVIHRNDW 


VNVKD

« Hide

References

« Hide 'large scale' references
[1]"Multiple copies of the proB gene enhance degS-dependent extracellular protease production in Bacillus subtilis."
Ogura M., Kawata-Mukai M., Itaya M., Takio K., Tanaka T.
J. Bacteriol. 176:5673-5680(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.
Strain: 168.
[2]"Sequence of the Bacillus subtilis genome between xlyA and ykoR."
Devine K.M.
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[3]"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. expand/collapse author list , 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.
[4]"From a consortium sequence to a unified sequence: the Bacillus subtilis 168 reference genome a decade later."
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.
Microbiology 155:1758-1775(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION TO 51 AND 54.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D26044 Genomic DNA. Translation: BAA05044.1.
AJ002571 Genomic DNA. Translation: CAA05591.1.
AL009126 Genomic DNA. Translation: CAB13169.2.
PIRD69682.
RefSeqNP_389195.2. NC_000964.3.

3D structure databases

ProteinModelPortalP39820.
SMRP39820. Positions 2-362.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU13120.

Proteomic databases

PaxDbP39820.

Protocols and materials databases

DNASU936790.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13169; CAB13169; BSU13120.
GeneID936790.
KEGGbsu:BSU13120.
PATRIC18974381. VBIBacSub10457_1383.

Organism-specific databases

GenoListBSU13120. [Micado]

Phylogenomic databases

eggNOGCOG0263.
HOGENOMHOG000246369.
KOK00931.
ProtClustDBPRK05429.

Enzyme and pathway databases

BioCycBSUB:BSU13120-MONOMER.
UniPathwayUPA00098; UER00359.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
HAMAPMF_00456. ProB.
InterProIPR001048. 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]
PfamPF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]
PIRSFPIRSF000729. GK. 1 hit.
PRINTSPR00474. GLU5KINASE.
SMARTSM00359. PUA. 1 hit.
[Graphical view]
SUPFAMSSF53633. Aa_kinase. 1 hit.
SSF88697. PUA-like. 1 hit.
TIGRFAMsTIGR01027. proB. 1 hit.
PROSITEPS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePROB_BACSU
AccessionPrimary (citable) accession number: P39820
Secondary accession number(s): O34562
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 16, 2009
Last modified: May 1, 2013
This is version 101 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents