UniProtKB - P0A039 (GLN1A_STAAW)
(max 400 entries)x
Your basket is currently empty. i
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
Protein
Glutamine synthetase
Gene
glnA
Organism
Staphylococcus aureus (strain MW2)
Status
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 | Graphical view | 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
GO - Biological processi
- glutamine biosynthetic process Source: InterPro
- nitrogen fixation Source: InterPro
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 | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › |
Proteomesi |
|
Subcellular locationi
- Cytoplasm By similarity
GO - Cellular componenti
- cytoplasm Source: UniProtKB-SubCell
Keywords - Cellular componenti
CytoplasmPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000153263 | 1 – 446 | Glutamine synthetaseAdd BLAST | 446 |
Proteomic databases
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. |
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. |
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. |
i Sequence
Sequence statusi: Complete.
P0A039-1 [UniParc]FASTAAdd to basket
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
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000033 Genomic DNA. Translation: BAB95057.1. |
RefSeqi | WP_001126603.1. NC_003923.1. |
Genome annotation databases
EnsemblBacteriai | BAB95057; BAB95057; BAB95057. |
KEGGi | sam:MW1192. |
Similar proteinsi
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 |