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P12425

- GLNA_BACSU

UniProt

P12425 - GLNA_BACSU

Protein

Glutamine synthetase

Gene

glnA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Enzyme regulationi

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

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. glutamate-ammonia ligase activity Source: UniProtKB-EC
    3. protein binding Source: IntAct

    GO - Biological processi

    1. glutamine biosynthetic process Source: CACAO
    2. nitrogen fixation Source: InterPro

    Keywords - Molecular functioni

    Ligase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciBSUB:BSU17460-MONOMER.
    SABIO-RKP12425.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamine synthetase (EC:6.3.1.2)
    Alternative name(s):
    Glutamate--ammonia ligase
    Gene namesi
    Name:glnA
    Ordered Locus Names:BSU17460
    OrganismiBacillus subtilis (strain 168)
    Taxonomic identifieri224308 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
    ProteomesiUP000001570: Chromosome

    Organism-specific databases

    GenoListiBSU17460. [Micado]

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 444443Glutamine synthetasePRO_0000153233Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei373 – 3731O-AMP-tyrosineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP12425.

    Expressioni

    Inductioni

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

    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. This inhibitory effect is the highest when both glutamine and AMP are present.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    tnrAQ456668EBI-6402863,EBI-8507041

    Protein-protein interaction databases

    DIPiDIP-29670N.
    IntActiP12425. 4 interactions.
    MINTiMINT-224371.
    STRINGi224308.BSU17460.

    Structurei

    Secondary structure

    1
    444
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi6 – 1611
    Beta strandi20 – 267
    Beta strandi32 – 387
    Helixi39 – 413
    Helixi42 – 465
    Beta strandi51 – 533
    Helixi54 – 563
    Helixi63 – 653
    Beta strandi67 – 8014
    Helixi81 – 833
    Helixi84 – 874
    Beta strandi89 – 979
    Beta strandi99 – 1035
    Helixi108 – 12114
    Beta strandi125 – 1339
    Beta strandi135 – 1406
    Beta strandi142 – 1443
    Beta strandi146 – 1516
    Turni160 – 1623
    Beta strandi163 – 1653
    Helixi166 – 17813
    Beta strandi183 – 1886
    Beta strandi194 – 1996
    Helixi204 – 22421
    Beta strandi227 – 2304
    Beta strandi244 – 2529
    Beta strandi261 – 2633
    Helixi264 – 2663
    Helixi269 – 28921
    Helixi295 – 2984
    Beta strandi311 – 3133
    Beta strandi316 – 3227
    Helixi327 – 3293
    Beta strandi332 – 3343
    Helixi343 – 35917
    Helixi372 – 3743
    Helixi377 – 3837
    Helixi392 – 4009
    Helixi403 – 4097
    Helixi411 – 43020
    Helixi434 – 4407
    Turni441 – 4433

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliP12425.
    SMRiP12425. Positions 5-443.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glutamine synthetase family.Curated

    Phylogenomic databases

    eggNOGiCOG0174.
    HOGENOMiHOG000005156.
    KOiK01915.
    OMAiIEWDMFR.
    OrthoDBiEOG6B360N.
    PhylomeDBiP12425.

    Family and domain databases

    Gene3Di3.10.20.70. 1 hit.
    3.30.590.10. 1 hit.
    InterProiIPR008147. 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]
    PfamiPF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF54368. SSF54368. 1 hit.
    TIGRFAMsiTIGR00653. GlnA. 1 hit.
    PROSITEiPS00180. GLNA_1. 1 hit.
    PS00182. GLNA_ADENYLATION. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P12425-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAKYTREDIE KLVKEENVKY IRLQFTDILG TIKNVEIPVS QLGKALDNKV    50
    MFDGSSIEGF VRIEESDMYL YPDLNTFVIF PWTAEKGKVA RFICDIYNPD 100
    GTPFEGDPRN NLKRILKEME DLGFSDFNLG PEPEFFLFKL DEKGEPTLEL 150
    NDKGGYFDLA PTDLGENCRR DIVLELEEMG FEIEASHHEV APGQHEIDFK 200
    YAGAVRSCDD IQTFKLVVKT IARKHGLHAT FMPKPLFGVN GSGMHCNLSL 250
    FKNGVNAFFD ENADLQLSET AKHFIAGIVK HATSFTAVTN PTVNSYKRLV 300
    PGYEAPCYVA WSAQNRSPLI RIPASRGIST RVEVRSVDPA ANPYLALSVL 350
    LAAGLDGIKN KLEAPAPIDR NIYVMSKEER MENGIVDLPA TLAEALEEFK 400
    SNEVMVKALG EHLFEHFIEA KEIEWDMFRT QVHPWEREQY MSQY 444
    Length:444
    Mass (Da):50,278
    Last modified:January 23, 2007 - v3
    Checksum:i83A5657CE1388AB0
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti10 – 101E → V in strain: PCI 219.
    Natural varianti43 – 431G → E in strain: PCI 219.
    Natural varianti253 – 2531N → D in strain: PCI 219.
    Natural varianti259 – 2591F → Y in strain: PCI 219.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22811 Genomic DNA. Translation: AAA83376.1.
    D00854 Genomic DNA. Translation: BAA00730.1.
    U66480 Genomic DNA. Translation: AAB41080.1.
    AL009126 Genomic DNA. Translation: CAB13630.1.
    PIRiJT0392. AJBSQS.
    RefSeqiNP_389628.1. NC_000964.3.
    WP_003231737.1. NZ_CM000487.1.

    Genome annotation databases

    EnsemblBacteriaiCAB13630; CAB13630; BSU17460.
    GeneIDi940020.
    KEGGibsu:BSU17460.
    PATRICi18975307. VBIBacSub10457_1845.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22811 Genomic DNA. Translation: AAA83376.1 .
    D00854 Genomic DNA. Translation: BAA00730.1 .
    U66480 Genomic DNA. Translation: AAB41080.1 .
    AL009126 Genomic DNA. Translation: CAB13630.1 .
    PIRi JT0392. AJBSQS.
    RefSeqi NP_389628.1. NC_000964.3.
    WP_003231737.1. NZ_CM000487.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2FWX model - A/B/C/D 1-444 [» ]
    3QAJ X-ray 3.05 A/B/C/D/E/F/G/H/I/J/K/L 1-444 [» ]
    4LNF X-ray 2.95 A/B/C/D/E/F/G/H/I/J/K/L 2-444 [» ]
    4LNI X-ray 2.58 A/B/C/D/E/F/G/H/I/J/K/L 2-444 [» ]
    4LNK X-ray 2.87 A/B/C/D/E/F 2-444 [» ]
    4LNN X-ray 3.10 A/B/C/D/E/F/G/H/I/J/K/L 2-444 [» ]
    4LNO X-ray 2.90 A/B/C/D/E/F 2-444 [» ]
    ProteinModelPortali P12425.
    SMRi P12425. Positions 5-443.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29670N.
    IntActi P12425. 4 interactions.
    MINTi MINT-224371.
    STRINGi 224308.BSU17460.

    Proteomic databases

    PaxDbi P12425.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAB13630 ; CAB13630 ; BSU17460 .
    GeneIDi 940020.
    KEGGi bsu:BSU17460.
    PATRICi 18975307. VBIBacSub10457_1845.

    Organism-specific databases

    GenoListi BSU17460. [Micado ]

    Phylogenomic databases

    eggNOGi COG0174.
    HOGENOMi HOG000005156.
    KOi K01915.
    OMAi IEWDMFR.
    OrthoDBi EOG6B360N.
    PhylomeDBi P12425.

    Enzyme and pathway databases

    BioCyci BSUB:BSU17460-MONOMER.
    SABIO-RK P12425.

    Family and domain databases

    Gene3Di 3.10.20.70. 1 hit.
    3.30.590.10. 1 hit.
    InterProi IPR008147. 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 ]
    Pfami PF00120. Gln-synt_C. 1 hit.
    PF03951. Gln-synt_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54368. SSF54368. 1 hit.
    TIGRFAMsi TIGR00653. GlnA. 1 hit.
    PROSITEi PS00180. GLNA_1. 1 hit.
    PS00182. GLNA_ADENYLATION. 1 hit.
    PS00181. GLNA_ATP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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.

    Entry informationi

    Entry nameiGLNA_BACSU
    AccessioniPrimary (citable) accession number: P12425
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 125 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Bacillus subtilis
      Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3