Reviewed, UniProtKB/Swiss-Prot Q9PJ29 (PROB_CAMJE)

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 [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	251 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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. HAMAP MF_00456
Catalytic activity	ATP + L-glutamate = ADP + L-glutamate 5-phosphate. HAMAP MF_00456
Pathway	Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-glutamate: step 1/2. HAMAP 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
Gene Ontology (GO)
Biological process	proline biosynthetic process Inferred from electronic annotation. Source: HAMAP
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 protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
fliY	Q0PC74	1	EBI-1192821,EBI-1191111

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 251

251

Glutamate 5-kinase HAMAP MF_00456

PRO_0000109656

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)
	Q9PJ29-1 [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

[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: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AL111168 Genomic DNA. Translation: CAL34268.1.

PIR

A81426.

RefSeq

YP_002343557.1.

3D structure databases

PDBPDBe

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

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9PJ29. 10 interactions.

Genome annotation databases

GeneID

904426.

GenomeReviews

Gene locus Cj0097 in contig AL111168_GR.

KEGG

cje:Cj0097.

Organism-specific databases

CMR

Search...

Phylogenomic databases

OMA

Q9PJ29. NENDVIA.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ0097-MON.

BRENDA

2.7.2.11. 255835.

Family and domain databases

HAMAP

MF_00456.
[Tree]

InterPro

IPR001048. Asp/Glu/Uridylate_kinase.
IPR001057. Glu_5kinase.
IPR011529. Glu_5kinase_bact.
IPR019797. Glutamate_5-kinase_CS.
IPR005715. ProB.
[Graphical view]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.

Pfam

PF00696. AA_kinase. 1 hit.
[Graphical view]

PIRSF

PIRSF000729. GK. 1 hit.

PRINTS

PR00474. GLU5KINASE.

TIGRFAMs

TIGR01027. proB. 1 hit.

PROSITE

PS00902. GLUTAMATE_5_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

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:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)