Q93Q56 (PROB_LISMO) 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:	lmo1260

Organism

Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) [Reference proteome] [HAMAP]

Taxonomic identifier

169963 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Listeriaceae › Listeria › Listeria monocytogenes

Protein attributes

Sequence length	276 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

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	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 – 276	276	Glutamate 5-kinase HAMAP-Rule MF_00456		PRO_0000109689
Regions
	Nucleotide binding	177 – 178	2	ATP By similarity
	Nucleotide binding	219 – 225	7	ATP By similarity
Sites
	Binding site	14	1	ATP By similarity
	Binding site	54	1	Substrate By similarity
	Binding site	141	1	Substrate By similarity
	Binding site	157	1	Substrate; via amide nitrogen By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q93Q56 [UniParc]. Last modified December 1, 2001. Version 1. Checksum: F9A94811AFC5AD06	FASTA	276	30,034
	10 20 30 40 50 60 MRESLKNSKR LVIKVGTSTL MYGNGHINLR TIEKLAMVLS DLRNEGKEVI LVSSGAIGVG 70 80 90 100 110 120 CHKLQLPVRP TSIPEQQAVA SVGQSELMHI YSKFFGEYGQ VVGQVLLTRD VTDFPISREN 130 140 150 160 170 180 VMNTLESLLE RGIIPIVNEN DTVAVEELEH VTKYGDNDLL SAIVAKLVQA DLLIMLSDID 190 200 210 220 230 240 GFYGSNPSTD PDAVMFSEIN QITPEIEALA GGKGSKFGTG GMLTKLSAAS YCMNANQKMI 250 260 270 LTNGKNPTII FDIMQGEQIG TLFASKKEEF SHDGTH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and disruption of the proBA Locus in Listeria monocytogenes: role of proline biosynthesis in salt tolerance and murine infection." Sleator R.D., Gahan C.G.M., Hill C. Appl. Environ. Microbiol. 67:2571-2577(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. , Durant L., Dussurget O., Entian K.-D., Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A., Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B., Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P. Science 294:849-852(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-679 / EGD-e.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF282880 Genomic DNA. Translation: AAK62254.1. AL591978 Genomic DNA. Translation: CAC99338.1.
PIR	AD1232.
RefSeq	NP_464785.1. NC_003210.1.
3D structure databases
ProteinModelPortal	Q93Q56.
ModBase	Search...
Protein-protein interaction databases
STRING	169963.lmo1260.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAC99338; CAC99338; CAC99338.
GeneID	985996.
KEGG	lmo:lmo1260.
PATRIC	20311637. VBILisMon69206_1295.
Organism-specific databases
GenoList	LMO1260.
Phylogenomic databases
eggNOG	COG0263.
HOGENOM	HOG000246368.
KO	K00931.
OMA	VYTGNPK.
ProtClustDB	PRK12314.
Enzyme and pathway databases
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...

Entry information

Entry name

PROB_LISMO

Accession

Primary (citable) accession number: Q93Q56

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 6, 2002
Last sequence update:	December 1, 2001
Last modified:	May 1, 2013
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program