Q9PJ29 (PROB_CAMJE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Glutamate 5-kinase
EC=2.7.2.11

Alternative name(s):
Gamma-glutamyl kinase
Short name=GK

Gene names

Name:	proB
Ordered Locus Names:	Cj0097

Organism

Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168) [Reference proteome] [HAMAP]

Taxonomic identifier

192222 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › delta/epsilon subdivisions › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter › Campylobacter jejuni › Campylobacter jejuni subsp. jejuni

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Protein existence	Evidence 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 By similarity. 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.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Proline biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	L-proline biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW glutamate 5-kinase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 251

251

Glutamate 5-kinase HAMAP-Rule MF_00456

PRO_0000109656

Regions

Nucleotide binding

162 – 163

2

ATP HAMAP-Rule MF_00456

Nucleotide binding

168 – 173

6

ATP HAMAP-Rule MF_00456

Nucleotide binding

204 – 210

7

ATP HAMAP-Rule MF_00456

Sites

Binding site

7

1

ATP By similarity

Binding site

45

1

Substrate By similarity

Binding site

130

1

Substrate By similarity

Binding site

142

1

Substrate; via amide nitrogen By similarity

Secondary structure

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251

Helix Strand Turn

Details...

Beta strand

3 – 8

6

Helix

10 – 13

4

Beta strand

16 – 19

4

Helix

21 – 37

17

Beta strand

38 – 44

7

Helix

47 – 54

8

Beta strand

59 – 61

3

Helix

62 – 84

23

Helix

85 – 87

3

Beta strand

91 – 96

6

Helix

99 – 102

4

Helix

104 – 119

16

Beta strand

123 – 128

6

Turn

130 – 132

3

Helix

135 – 138

4

Turn

140 – 142

3

Helix

143 – 152

10

Beta strand

156 – 164

9

Beta strand

168 – 170

3

Turn

172 – 174

3

Beta strand

183 – 185

3

Helix

189 – 191

3

Helix

206 – 219

14

Beta strand

223 – 231

9

Helix

233 – 240

8

Beta strand

246 – 250

5

Sequences

	Sequence		Length	Mass (Da)
	Q9PJ29 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: D07802E92023A241	FASTA	251	27,843
	10 20 30 40 50 60 MKRIVVKVGS HVISEENTLS FERLKNLVAF LAKLMEKYEV ILVTSAAISA GHTKLDIDRK 70 80 90 100 110 120 NLINKQVLAA IGQPFLISVY NELLAKFNKL GGQILLTGKD FDSRKATKHA KNAIDMMINL 130 140 150 160 170 180 GILPIINEND ATAIEEIVFG DNDSLSAYAT HFFDADLLVI LSDIDGFYDK NPSEFSDAKR 190 200 210 220 230 240 LEKITHIKEE WLQATIKTGS EHGTGGIVTK LKAAKFLLEH NKKMFLASGF DLSVAKTFLL 250 EDKQIGGTLF E

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168.
[2]	"Crystal structure of glutamate 5-kinase from Campylobacter jejuni." Gorman J., Shapiro L. Submitted (AUG-2005) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH ADP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AL111168 Genomic DNA. Translation: CAL34268.1.

PIR

A81426.

RefSeq

YP_002343557.1. NC_002163.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2AKO	X-ray	2.20	A/B/C/D	1-251	[»]

ProteinModelPortal

Q9PJ29.

SMR

Q9PJ29. Positions 2-251.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9PJ29. 9 interactions.

STRING

192222.Cj0097.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

CAL34268; CAL34268; Cj0097.

GeneID

904426.

KEGG

cje:Cj0097.

PATRIC

20057121. VBICamJej33762_0095.

Phylogenomic databases

eggNOG

COG0263.

HOGENOM

HOG000246368.

KO

K00931.

OMA

FDFPSAQ.

ProtClustDB

PRK12314.

Enzyme and pathway databases

BioCyc

CJEJ192222:GJTS-93-MONOMER.

UniPathway

UPA00098; UER00359.

Family and domain databases

Gene3D

3.40.1160.10. 1 hit.

HAMAP

MF_00456. ProB.

InterPro

IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu/AcGlu_kinase.
IPR011529. Glu_5kinase.
IPR005715. Glu_5kinase/COase_Synthase.
IPR019797. Glutamate_5-kinase_CS.
[Graphical view]

Pfam

PF00696. AA_kinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000729. GK. 1 hit.

PRINTS

PR00474. GLU5KINASE.

SUPFAM

SSF53633. Aa_kinase. 1 hit.

TIGRFAMs

TIGR01027. proB. 1 hit.

PROSITE

PS00902. GLUTAMATE_5_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9PJ29.

Entry information

Entry name

PROB_CAMJE

Accession

Primary (citable) accession number: Q9PJ29
Secondary accession number(s): Q0PC40

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 26, 2001
Last sequence update:	October 1, 2000
Last modified:	May 1, 2013
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program