glnA

Functionⁱ

Glutamine synthetase (GS) is an unusual multitasking protein that functions as an enzyme, a transcription coregulator, and a chaperone in ammonium assimilation and in the regulation of genes involved in nitrogen metabolism. It catalyzes the ATP-dependent biosynthesis of glutamine from glutamate and ammonia. Feedback-inhibited GlnA also interacts with and regulates the activity of the transcriptional regulator TnrA. During nitrogen limitation, TnrA is in its DNA-binding active state and turns on the transcription of genes required for nitrogen assimilation. Under conditions of nitrogen excess, feedback-inhibited GlnA forms a stable complex with TnrA, which inhibits its DNA-binding activity. In contrast, feedback-inhibited GlnA acts as a chaperone to stabilize the DNA-binding activity of GlnR, which represses the transcription of nitrogen assimilation genes.By similarity

Catalytic activityⁱ

ATP + L-glutamate + NH₃ = ADP + phosphate + L-glutamine.By similarity

Cofactorⁱ

Mg²⁺By similarityNote: Binds 2 Mg²⁺ ions per subunit.By similarity

Enzyme regulationⁱ

Inhibited by glutamine.By similarity

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	64	Important for inhibition by glutamineBy similarity	1
Metal bindingⁱ	134	Magnesium 1By similarity	1
Metal bindingⁱ	136	Magnesium 2By similarity	1
Binding siteⁱ	186	ATPBy similarity	1
Metal bindingⁱ	191	Magnesium 2By similarity	1
Metal bindingⁱ	198	Magnesium 2By similarity	1
Binding siteⁱ	243	L-glutamate; via carbonyl oxygenBy similarity	1
Metal bindingⁱ	247	Magnesium 1; via pros nitrogenBy similarity	1
Binding siteⁱ	251	ATPBy similarity	1
Binding siteⁱ	300	L-glutamateBy similarity	1
Binding siteⁱ	306	L-glutamateBy similarity	1
Binding siteⁱ	318	ATPBy similarity	1
Binding siteⁱ	318	L-glutamateBy similarity	1
Binding siteⁱ	323	ATPBy similarity	1
Metal bindingⁱ	335	Magnesium 1By similarity	1
Binding siteⁱ	337	L-glutamateBy similarity	1

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW
glutamate-ammonia ligase activity Source: UniProtKB-EC
metal ion binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

glutamine biosynthetic process Source: InterPro
nitrogen fixation Source: InterPro

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Ligase
Ligand	ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Glutamine synthetaseBy similarity (EC:6.3.1.2By similarity) Short name: GSBy similarity Alternative name(s): Glutamate--ammonia ligaseBy similarity Glutamine synthetase I alphaBy similarity Short name: GSI alphaBy similarity
Gene namesⁱ	Name:glnABy similarity Ordered Locus Names:MW1192
Organismⁱ	Staphylococcus aureus (strain MW2)
Taxonomic identifierⁱ	196620 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Terrabacteria group › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus
Proteomesⁱ	UP000000418 Componentⁱ: Chromosome

Subcellular locationⁱ

Cytoplasm
By similarity
Manual assertion inferred from sequence similarity toⁱ
- UniProtKB:P12425 (GLN1A_BACSU)

GO - Cellular componentⁱ

cytoplasm Source: UniProtKB-SubCell

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cytoplasm

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000153263	1 – 446	Glutamine synthetaseAdd BLAST		446

Proteomic databases

PRIDEⁱ	P0A039.

PRIDEⁱ

P0A039.

Interactionⁱ

Subunit structureⁱ

Oligomer of 12 subunits arranged in the form of two hexagons. In its feedback-inhibited form, interacts with TnrA in order to block its DNA-binding activity.By similarity

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P0A039.
SMRⁱ	P0A039.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Regionⁱ	242 – 243	L-glutamate bindingBy similarity		2

Sequence similaritiesⁱ

Belongs to the glutamine synthetase family.Curated

Phylogenomic databases

HOGENOMⁱ	HOG000005156.
KEGG Orthology (KO) More...KOⁱ	K01915.
OMAⁱ	IEAAWNT.

Family and domain databases

Gene3Dⁱ	3.10.20.70. 1 hit.
InterProⁱ	View protein in InterPro IPR008147. Gln_synt_b-grasp. IPR036651. Gln_synt_N. IPR014746. Gln_synth/guanido_kin_cat_dom. IPR008146. Gln_synth_cat_dom. IPR027303. Gln_synth_gly_rich_site. IPR004809. Gln_synth_I. IPR027302. Gln_synth_N_conserv_site.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00120. Gln-synt_C. 1 hit. PF03951. Gln-synt_N. 1 hit.
SMARTⁱ	View protein in SMART SM01230. Gln-synt_C. 1 hit.
SUPFAMⁱ	SSF54368. SSF54368. 1 hit. SSF55931. SSF55931. 1 hit.
TIGRFAMsⁱ	TIGR00653. GlnA. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00180. GLNA_1. 1 hit. PS00181. GLNA_ATP. 1 hit.

Sequenceⁱ

Sequence statusⁱ: Complete.

P0A039-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPKRTFTKDD IRKFAEEENV RYLRLQFTDI LGTIKNVEVP VSQLEKVLDN 
        60         70         80         90        100
EMMFDGSSIE GFVRIEESDM YLHPDLDTWV IFPWTAGQGK VARLICDVYK 
       110        120        130        140        150
TDGTPFEGDP RANLKRVLKE MEDLGFTDFN LGPEPEFFLF KLDEKGEPTL 
       160        170        180        190        200
ELNDDGGYFD LAPTDLGENC RRDIVLELED MGFDIEASHH EVAPGQHEID 
       210        220        230        240        250
FKYADAVTAC DNIQTFKLVV KTIARKHNLH ATFMPKPLFG VNGSGMHFNV 
       260        270        280        290        300
SLFKGKENAF FDPNTEMGLT ETAYQFTAGV LKNARGFTAV CNPLVNSYKR 
       310        320        330        340        350
LVPGYEAPCY IAWSGKNRSP LIRVPSSRGL STRIEVRSVD PAANPYMALA 
       360        370        380        390        400
AILEAGLDGI KNKLKVPEPV NQNIYEMNRE EREAVGIQDL PSTLYTALKA 
       410        420        430        440 
MRENEVIKKA LGNHIYNQFI NSKSIEWDYY RTQVSEWERD QYMKQY

Length:446

Mass (Da):50,841

Last modified:February 15, 2005 - v1

Checksum:ⁱ81713EE654D7E7E6

GO

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BA000033 Genomic DNA. Translation: BAB95057.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_001126603.1. NC_003923.1.

Genome annotation databases

EnsemblBacteriaⁱ	BAB95057; BAB95057; BAB95057.
KEGGⁱ	sam:MW1192.

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P0A039	Q5HGC3 Q6G9Q4 P0A040 A0A2K4ADX3 A0A077VWZ5 A0A0D1JX26 G7ZN56 A0A0E1AFZ2 A0A0E1VK00 Q2FYY6 +13	Staphylococcus aureus (strain COL) Staphylococcus aureus (strain MSSA476) Staphylococcus aureus Staphylococcus schweitzeri Staphylococcus aureus subsp. aureus Staphylococcus argenteus Staphylococcus aureus subsp. aureus Z172 Staphylococcus aureus subsp. aureus USA300_TCH959 Staphylococcus aureus (strain NCTC 8325) Staphylococcus aureus O46 And more	446	UniRef100_Q5HGC3	Cluster: Glutamine synthetase	24

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P0A039	P60890 P99095 E3VXC2 UPI000B962D9E A0A2K3V7P3 Q4L616 A0A1F2KVC3 A0A1N4TZ71 A0A1U0WHW6 A0A2K4D5J6 +231	Staphylococcus aureus (strain Mu50 / ATCC 700699) Staphylococcus aureus (strain N315) Staphylococcus aureus Staphylococcus haemolyticus Staphylococcus haemolyticus (strain JCSC1435) Staphylococcus sp. HMSC14D01 Mycobacterium abscessus subsp. abscessus Staphylococcus hominis subsp. novobiosepticus Streptococcus pneumoniae Staphylococcus sp. HMSC078E07 And more	446	UniRef90_P60890	Cluster: Glutamine synthetase	242

Protein	Similar proteins	Organisms	Length	Cluster ID	Cluster name	Size
P0A039	P12425 A0A085CCI2 A0A1B2AWL5 G4EVZ4 A0A1X7FIS9 A0A125UIF4 L8AID0 M4KRP2 A0A285L5A4 UPI0005CDCEF6 +1239	Bacillus subtilis (strain 168) Bacillus subtilis Bacillus subtilis subsp. subtilis Bacillus subtilis subsp. subtilis str. SC-8 Bacillus sp. CC120222-01 Bacillus sp. LM 4-2 Bacillus subtilis BEST7613 Bacillus subtilis XF-1 Bacillus sp. GL120224-02 Streptococcus pneumoniae And more	444	UniRef50_P12425	Cluster: Glutamine synthetase	1,250

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	BA000033 Genomic DNA. Translation: BAB95057.1.
NCBI Reference Sequences More...RefSeqⁱ	WP_001126603.1. NC_003923.1.

3D structure databases

ProteinModelPortalⁱ	P0A039.
SMRⁱ	P0A039.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Proteomic databases

PRIDEⁱ	P0A039.

PRIDEⁱ

P0A039.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	BAB95057; BAB95057; BAB95057.
KEGGⁱ	sam:MW1192.

Phylogenomic databases

HOGENOMⁱ	HOG000005156.
KEGG Orthology (KO) More...KOⁱ	K01915.
OMAⁱ	IEAAWNT.

Family and domain databases

Gene3Dⁱ	3.10.20.70. 1 hit.
InterProⁱ	View protein in InterPro IPR008147. Gln_synt_b-grasp. IPR036651. Gln_synt_N. IPR014746. Gln_synth/guanido_kin_cat_dom. IPR008146. Gln_synth_cat_dom. IPR027303. Gln_synth_gly_rich_site. IPR004809. Gln_synth_I. IPR027302. Gln_synth_N_conserv_site.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00120. Gln-synt_C. 1 hit. PF03951. Gln-synt_N. 1 hit.
SMARTⁱ	View protein in SMART SM01230. Gln-synt_C. 1 hit.
SUPFAMⁱ	SSF54368. SSF54368. 1 hit. SSF55931. SSF55931. 1 hit.
TIGRFAMsⁱ	TIGR00653. GlnA. 1 hit.
PROSITEⁱ	View protein in PROSITE PS00180. GLNA_1. 1 hit. PS00181. GLNA_ATP. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	GLN1A_STAAW
Accessionⁱ	P0A039Primary (citable) accession number: P0A039 Secondary accession number(s): Q59812
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	February 15, 2005
	Last sequence update:	February 15, 2005
	Last modified:	March 28, 2018
	This is version 79 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome

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UniParc

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Annotation systems

Supporting data

UniProtKB - P0A039 (GLN1A_STAAW)

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Glutamine synthetase

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi

Sites

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Sequence databases

Genome annotation databases

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Sequence databases

3D structure databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

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Functionⁱ

Enzyme regulationⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

PTM / Processingⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ