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P0A040

- GLNA_STAAU

UniProt

P0A040 - GLNA_STAAU

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Protein
Glutamine synthetase
Gene
glnA
Organism
Staphylococcus aureus
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

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.

GO - Molecular functioni

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

GO - Biological processi

  1. glutamine biosynthetic process Source: InterPro
  2. nitrogen fixation Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Glutamine synthetase (EC:6.3.1.2)
Short name:
GS
Alternative name(s):
Glutamate--ammonia ligase
Gene namesi
Name:glnA
OrganismiStaphylococcus aureus
Taxonomic identifieri1280 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 446446Glutamine synthetase
PRO_0000153262Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei375 – 3751O-AMP-tyrosine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiP0A040.

Interactioni

Subunit structurei

Oligomer of 12 subunits arranged in the form of two hexagons By similarity.

Structurei

3D structure databases

ProteinModelPortaliP0A040.
SMRiP0A040. Positions 6-446.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0174.

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.
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.
PS00181. GLNA_ATP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0A040-1 [UniParc]FASTAAdd to Basket

« Hide

MPKRTFTKDD IRKFAEEENV RYLRLQFTDI LGTIKNVEVP VSQLEKVLDN    50
EMMFDGSSIE GFVRIEESDM YLHPDLDTWV IFPWTAGQGK VARLICDVYK 100
TDGTPFEGDP RANLKRVLKE MEDLGFTDFN LGPEPEFFLF KLDEKGEPTL 150
ELNDDGGYFD LAPTDLGENC RRDIVLELED MGFDIEASHH EVAPGQHEID 200
FKYADAVTAC DNIQTFKLVV KTIARKHNLH ATFMPKPLFG VNGSGMHFNV 250
SLFKGKENAF FDPNTEMGLT ETAYQFTAGV LKNARGFTAV CNPLVNSYKR 300
LVPGYEAPCY IAWSGKNRSP LIRVPSSRGL STRIEVRSVD PAANPYMALA 350
AILEAGLDGI KNKLKVPEPV NQNIYEMNRE EREAVGIQDL PSTLYTALKA 400
MRENEVIKKA LGNHIYNQFI NSKSIEWDYY RTQVSEWERD QYMKQY 446
Length:446
Mass (Da):50,841
Last modified:February 15, 2005 - v1
Checksum:i81713EE654D7E7E6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76490 Genomic DNA. Translation: CAA54030.1.
PIRiT51803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X76490 Genomic DNA. Translation: CAA54030.1 .
PIRi T51803.

3D structure databases

ProteinModelPortali P0A040.
SMRi P0A040. Positions 6-446.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PRIDEi P0A040.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG0174.

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.
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.
PS00181. GLNA_ATP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Glutamine synthetase and heteroresistance in methicillin-resistant Staphylococcus aureus."
    Stranden A.M., Roos M., Berger-Baechi B.
    Microb. Drug Resist. 2:201-207(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BB270 / AS63.

Entry informationi

Entry nameiGLNA_STAAU
AccessioniPrimary (citable) accession number: P0A040
Secondary accession number(s): Q59812
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 15, 2005
Last sequence update: February 15, 2005
Last modified: September 3, 2014
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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