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P12425 (GLNA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glutamine synthetase

EC=6.3.1.2
Alternative name(s):
Glutamate--ammonia ligase
Gene names
Name:glnA
Ordered Locus Names:BSU17460
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

The activity of this enzyme is controlled by adenylation under conditions of abundant glutamine. The fully adenylated enzyme complex is inactive By similarity.

Subunit structure

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. This inhibitory effect is the highest when both glutamine and AMP are present. Ref.5

Subcellular location

Cytoplasm.

Induction

Repressed by GlnR under conditions of nitrogen excess. Repressed by TnrA under conditions of nitrogen limitation.

Miscellaneous

Elevated Mn2+ concentration reduces sensitivity of GlnA to feedback inhibitors Gln and AMP.

Sequence similarities

Belongs to the glutamine synthetase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

tnrAQ456668EBI-6402863,EBI-8507041

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 444443Glutamine synthetase
PRO_0000153233

Amino acid modifications

Modified residue3731O-AMP-tyrosine By similarity

Natural variations

Natural variant101E → V in strain: PCI 219.
Natural variant431G → E in strain: PCI 219.
Natural variant2531N → D in strain: PCI 219.
Natural variant2591F → Y in strain: PCI 219.

Secondary structure

............................................................................ 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12425 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 83A5657CE1388AB0

FASTA44450,278
        10         20         30         40         50         60 
MAKYTREDIE KLVKEENVKY IRLQFTDILG TIKNVEIPVS QLGKALDNKV MFDGSSIEGF 

        70         80         90        100        110        120 
VRIEESDMYL YPDLNTFVIF PWTAEKGKVA RFICDIYNPD GTPFEGDPRN NLKRILKEME 

       130        140        150        160        170        180 
DLGFSDFNLG PEPEFFLFKL DEKGEPTLEL NDKGGYFDLA PTDLGENCRR DIVLELEEMG 

       190        200        210        220        230        240 
FEIEASHHEV APGQHEIDFK YAGAVRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLFGVN 

       250        260        270        280        290        300 
GSGMHCNLSL FKNGVNAFFD ENADLQLSET AKHFIAGIVK HATSFTAVTN PTVNSYKRLV 

       310        320        330        340        350        360 
PGYEAPCYVA WSAQNRSPLI RIPASRGIST RVEVRSVDPA ANPYLALSVL LAAGLDGIKN 

       370        380        390        400        410        420 
KLEAPAPIDR NIYVMSKEER MENGIVDLPA TLAEALEEFK SNEVMVKALG EHLFEHFIEA 

       430        440 
KEIEWDMFRT QVHPWEREQY MSQY 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the Bacillus subtilis glutamine synthetase gene region."
Strauch M.A., Aronson A.I., Brown S.W., Schreier H.J., Sonenshein A.L.
Gene 71:257-265(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete nucleotide sequence of the glutamine synthetase gene (glnA) of Bacillus subtilis."
Nakano Y., Tanaka E., Kato C., Kimura K., Horikoshi K.
FEMS Microbiol. Lett. 48:81-86(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21.
Strain: ATCC 6633 / PCI 219 / NRS 231.
[3]"Sequencing of a 26 kb region of the Bacillus subtilis genome downstream of spoVJ."
Borchert S., Klein C., Piksa B., Hammelmann M., Entian K.-D.
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"Bacillus subtilis glutamine synthetase controls gene expression through a protein-protein interaction with transcription factor TnrA."
Wray L.V. Jr., Zalieckas J.M., Fisher S.H.
Cell 107:427-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TNRA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M22811 Genomic DNA. Translation: AAA83376.1.
D00854 Genomic DNA. Translation: BAA00730.1.
U66480 Genomic DNA. Translation: AAB41080.1.
AL009126 Genomic DNA. Translation: CAB13630.1.
PIRAJBSQS. JT0392.
RefSeqNP_389628.1. NC_000964.3.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FWXmodel-A/B/C/D1-444[»]
3QAJX-ray3.05A/B/C/D/E/F/G/H/I/J/K/L1-444[»]
4LNFX-ray2.95A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNIX-ray2.58A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNKX-ray2.87A/B/C/D/E/F2-444[»]
4LNNX-ray3.10A/B/C/D/E/F/G/H/I/J/K/L2-444[»]
4LNOX-ray2.90A/B/C/D/E/F2-444[»]
ProteinModelPortalP12425.
SMRP12425. Positions 5-443.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29670N.
IntActP12425. 4 interactions.
MINTMINT-224371.
STRING224308.BSU17460.

Proteomic databases

PaxDbP12425.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB13630; CAB13630; BSU17460.
GeneID940020.
KEGGbsu:BSU17460.
PATRIC18975307. VBIBacSub10457_1845.

Organism-specific databases

GenoListBSU17460. [Micado]

Phylogenomic databases

eggNOGCOG0174.
HOGENOMHOG000005156.
KOK01915.
OMAIEWDMFR.
OrthoDBEOG6B360N.
PhylomeDBP12425.

Enzyme and pathway databases

BioCycBSUB:BSU17460-MONOMER.
SABIO-RKP12425.

Family and domain databases

Gene3D3.10.20.70. 1 hit.
3.30.590.10. 1 hit.
InterProIPR008147. Gln_synt_beta.
IPR014746. Gln_synth/guanido_kin_cat_dom.
IPR008146. Gln_synth_cat_dom.
IPR027303. Gln_synth_gly_rich_site.
IPR004809. Gln_synth_I.
IPR001637. Gln_synth_I_adenylation_site.
IPR027302. Gln_synth_N_conserv_site.
[Graphical view]
PfamPF00120. Gln-synt_C. 1 hit.
PF03951. Gln-synt_N. 1 hit.
[Graphical view]
SUPFAMSSF54368. SSF54368. 1 hit.
TIGRFAMsTIGR00653. GlnA. 1 hit.
PROSITEPS00180. GLNA_1. 1 hit.
PS00182. GLNA_ADENYLATION. 1 hit.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLNA_BACSU
AccessionPrimary (citable) accession number: P12425
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList