ID GLNA_STAAW Reviewed; 446 AA.
AC P0A039; Q59812;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 02-NOV-2016, entry version 72.
DE RecName: Full=Glutamine synthetase;
DE Short=GS;
DE EC=6.3.1.2;
DE AltName: Full=Glutamate--ammonia ligase;
GN Name=glnA; OrderedLocusNames=MW1192;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/S0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A.,
RA Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L.,
RA Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-
RT acquired MRSA.";
RL Lancet 359:1819-1827(2002).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate +
CC L-glutamine.
CC -!- ENZYME REGULATION: The activity of this enzyme is controlled by
CC adenylation under conditions of abundant glutamine. The fully
CC adenylated enzyme complex is inactive (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Oligomer of 12 subunits arranged in the form of two
CC hexagons. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the glutamine synthetase family.
CC {ECO:0000305}.
DR EMBL; BA000033; BAB95057.1; -; Genomic_DNA.
DR RefSeq; WP_001126603.1; NC_003923.1.
DR ProteinModelPortal; P0A039; -.
DR SMR; P0A039; -.
DR PRIDE; P0A039; -.
DR EnsemblBacteria; BAB95057; BAB95057; BAB95057.
DR GeneID; 28381131; -.
DR KEGG; sam:MW1192; -.
DR PATRIC; 19568980; VBIStaAur44266_1251.
DR HOGENOM; HOG000005156; -.
DR KO; K01915; -.
DR OMA; NIMTFRH; -.
DR Proteomes; UP000000418; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro.
DR Gene3D; 3.10.20.70; -; 1.
DR Gene3D; 3.30.590.10; -; 1.
DR InterPro; IPR008147; Gln_synt_b-grasp.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR InterPro; IPR008146; Gln_synth_cat_dom.
DR InterPro; IPR027303; Gln_synth_gly_rich_site.
DR InterPro; IPR004809; Gln_synth_I.
DR InterPro; IPR027302; Gln_synth_N_conserv_site.
DR Pfam; PF00120; Gln-synt_C; 1.
DR Pfam; PF03951; Gln-synt_N; 1.
DR SMART; SM01230; Gln-synt_C; 1.
DR SUPFAM; SSF54368; SSF54368; 1.
DR TIGRFAMs; TIGR00653; GlnA; 1.
DR PROSITE; PS00180; GLNA_1; 1.
DR PROSITE; PS00181; GLNA_ATP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding;
KW Phosphoprotein.
FT CHAIN 1 446 Glutamine synthetase.
FT /FTId=PRO_0000153263.
FT MOD_RES 375 375 O-AMP-tyrosine. {ECO:0000250}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 108 442 ipfam:Gln-synt_C [T]
FT MYHIT 19 100 ipfam:Gln-synt_N [T]
FT MYHIT 107 356 ismart:Gln-synt_C [T]
FT MYHIT 54 72 ipat:GLNA_1 [T]
FT MYHIT 236 251 ipat:GLNA_ATP [T]
SQ SEQUENCE 446 AA; 50841 MW; 81713EE654D7E7E6 CRC64;
MPKRTFTKDD IRKFAEEENV RYLRLQFTDI LGTIKNVEVP VSQLEKVLDN EMMFDGSSIE
GFVRIEESDM YLHPDLDTWV IFPWTAGQGK VARLICDVYK TDGTPFEGDP RANLKRVLKE
MEDLGFTDFN LGPEPEFFLF KLDEKGEPTL ELNDDGGYFD LAPTDLGENC RRDIVLELED
MGFDIEASHH EVAPGQHEID FKYADAVTAC DNIQTFKLVV KTIARKHNLH ATFMPKPLFG
VNGSGMHFNV SLFKGKENAF FDPNTEMGLT ETAYQFTAGV LKNARGFTAV CNPLVNSYKR
LVPGYEAPCY IAWSGKNRSP LIRVPSSRGL STRIEVRSVD PAANPYMALA AILEAGLDGI
KNKLKVPEPV NQNIYEMNRE EREAVGIQDL PSTLYTALKA MRENEVIKKA LGNHIYNQFI
NSKSIEWDYY RTQVSEWERD QYMKQY
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