P0A7B5 (PROB_ECOLI) 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:	b0242, JW0232

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	367 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. 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 HAMAP MF_00456.
Sequence similarities	Belongs to the glutamate 5-kinase family. Contains 1 PUA domain.

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 Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	proline biosynthetic process Inferred from mutant phenotype. Source: EcoCyc
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: InterPro glutamate 5-kinase activity Inferred from direct assay. Source: EcoCyc magnesium ion binding Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Glutamate 5-kinase HAMAP MF_00456

PRO_0000109669

Regions

Domain

275 – 353

79

PUA

Region

159 – 190

32

Role in the formation of carboxyl phosphates of amino acids Potential

Experimental info

Sequence conflict

143

1

E → A Ref.1

Sequence conflict

143

1

E → A Ref.2

Secondary structure

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367

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

13 – 16

4

Turn

17 – 19

3

Beta strand

20 – 22

3

Helix

25 – 40

16

Beta strand

44 – 49

6

Helix

52 – 60

9

Helix

69 – 92

24

Turn

93 – 95

3

Beta strand

98 – 103

6

Helix

105 – 108

4

Helix

111 – 126

16

Beta strand

130 – 135

6

Helix

142 – 144

3

Helix

149 – 160

12

Beta strand

163 – 169

7

Helix

215 – 226

12

Beta strand

230 – 235

6

Helix

241 – 247

7

Beta strand

252 – 255

4

Helix

264 – 270

7

Beta strand

277 – 280

4

Helix

282 – 291

10

Helix

297 – 299

3

Beta strand

300 – 305

6

Beta strand

312 – 317

6

Beta strand

322 – 327

6

Helix

332 – 338

7

Helix

343 – 345

3

Helix

346 – 350

5

Helix

361 – 363

3

Beta strand

364 – 366

3

Sequences

	Sequence		Length	Mass (Da)
	P0A7B5 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: 5541040202EBCCE8	FASTA	367	39,057
	10 20 30 40 50 60 MSDSQTLVVK LGTSVLTGGS RRLNRAHIVE LVRQCAQLHA AGHRIVIVTS GAIAAGREHL 70 80 90 100 110 120 GYPELPATIA SKQLLAAVGQ SRLIQLWEQL FSIYGIHVGQ MLLTRADMED RERFLNARDT 130 140 150 160 170 180 LRALLDNNIV PVINENDAVA TAEIKVGDND NLSALAAILA GADKLLLLTD QKGLYTADPR 190 200 210 220 230 240 SNPQAELIKD VYGIDDALRA IAGDSVSGLG TGGMSTKLQA ADVACRAGID TIIAAGSKPG 250 260 270 280 290 300 VIGDVMEGIS VGTLFHAQAT PLENRKRWIF GAPPAGEITV DEGATAAILE RGSSLLPKGI 310 320 330 340 350 360 KSVTGNFSRG EVIRICNLEG RDIAHGVSRY NSDALRRIAG HHSQEIDAIL GYEYGPVAVH RDDMITR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of the Escherichia coli proBA locus by DNA and protein sequencing." Deutch A.H., Rushlow K.E., Smith C.J. Nucleic Acids Res. 12:6337-6355(1984) [PubMed: 6089111] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-6 AND 8-12.
[2]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 143. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Complete nucleotide sequence of phoE, the structural gene for the phosphate limitation inducible outer membrane pore protein of Escherichia coli K12." Overbeeke N., Bergmans H., van Mansfeld F., Lugtenberg B. J. Mol. Biol. 163:513-532(1983) [PubMed: 6341601] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-62. Strain: K12.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X00786 Genomic DNA. Translation: CAA25363.1.
U70214 Genomic DNA. Translation: AAB08662.1.
U00096 Genomic DNA. Translation: AAC73346.1.
AP009048 Genomic DNA. Translation: BAA77911.2.
V00316 Genomic DNA. Translation: CAA23604.1.

PIR

KIECEG. C64749.

RefSeq

NP_414777.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2J5T	X-ray	2.90	A/B/C/D/E/F/G/H	1-367	[»]
2J5V	X-ray	2.50	A/B	1-367	[»]
2W21	X-ray	2.95	A	1-259	[»]

ProteinModelPortal

P0A7B5.

SMR

P0A7B5. Positions 3-367.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A7B5. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001715; EBESCP00000001715; EBESCG00000001413.
EBESCT00000016532; EBESCP00000015823; EBESCG00000015592.

GeneID

946425.

GenomeReviews

Gene locus JW0232 in contig AP009048_GR.
Gene locus b0242 in contig U00096_GR.

KEGG

ecj:JW0232.
eco:b0242.

PATRIC

32115599. VBIEscCol129921_0244.

Organism-specific databases

EchoBASE

EB0761.

EcoGene

EG10768. proB.

Phylogenomic databases

eggNOG

COG0263.

GeneTree

EBGT00050000011848.

HOGENOM

HBG507643.

OMA

TFGDNDM.

PhylomeDB

P0A7B5.

ProtClustDB

PRK05429.

Enzyme and pathway databases

BioCyc

EcoCyc:GLUTKIN-MONOMER.
MetaCyc:GLUTKIN-MONOMER.

BRENDA

2.7.2.11. 2026.

Gene expression databases

Genevestigator

P0A7B5.

Family and domain databases

HAMAP

MF_00456. ProB.
[Tree]

InterPro

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]

Gene3D

G3DSA:3.40.1160.10. Aa_kinase. 1 hit.

KO

K00931.

Pfam

PF00696. AA_kinase. 1 hit.
PF01472. PUA. 1 hit.
[Graphical view]

PIRSF

PIRSF000729. GK. 1 hit.

PRINTS

PR00474. GLU5KINASE.

SMART

SM00359. PUA. 1 hit.
[Graphical view]

SUPFAM

SSF53633. Aa_kinase. 1 hit.
SSF88697. PUA-like. 1 hit.

TIGRFAMs

TIGR01027. ProB. 1 hit.

PROSITE

PS00902. GLUTAMATE_5_KINASE. 1 hit.
PS50890. PUA. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PROB_ECOLI

Accession

Primary (citable) accession number: P0A7B5
Secondary accession number(s): P07005, P78293

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	June 7, 2005
Last modified:	January 25, 2012
This is version 65 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program