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Database: UniProt/TrEMBL
Entry: D5TE96_LEGP2
LinkDB: D5TE96_LEGP2
Original site: D5TE96_LEGP2 
ID   D5TE96_LEGP2            Unreviewed;       688 AA.
AC   D5TE96;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   16-APR-2014, entry version 19.
DE   RecName: Full=Glycine--tRNA ligase beta subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit;
GN   Name=glyS; OrderedLocusNames=lpa_02658;
OS   Legionella pneumophila serogroup 1 (strain 2300/99 Alcoy).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=423212;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2300/99 Alcoy;
RX   PubMed=20236513; DOI=10.1186/1471-2164-11-181;
RA   D'Auria G., Jimenez-Hernandez N., Peris-Bondia F., Moya A.,
RA   Latorre A.;
RT   "Legionella pneumophila pangenome reveals strain-specific virulence
RT   factors.";
RL   BMC Genomics 11:181-181(2010).
CC   -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate
CC       + glycyl-tRNA(Gly).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP001828; ADG25180.1; -; Genomic_DNA.
DR   RefSeq; YP_003619132.1; NC_014125.1.
DR   EnsemblBacteria; ADG25180; ADG25180; lpa_02658.
DR   GeneID; 9129715; -.
DR   KEGG; lpa:lpa_02658; -.
DR   PATRIC; 38181855; VBILegPne70474_2036.
DR   HOGENOM; HOG000264302; -.
DR   KO; K01879; -.
DR   BioCyc; LPNE423212:GHRR-1961-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:InterPro.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 1.10.730.10; -; 1.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR008909; DALR_anticod-bd.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   Pfam; PF05746; DALR_1; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
DR   SMART; SM00836; DALR_1; 1.
DR   TIGRFAMs; TIGR00211; glyS; 1.
DR   PROSITE; PS50861; AA_TRNA_LIGASE_II_GLYAB; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
SQ   SEQUENCE   688 AA;  76495 MW;  AFF61479E2B7AC46 CRC64;
     MVNDFIFELG CEELPSGAVW PLANEFSTRL LAALDKAQLS YGEVKRFATP RRLAIVIHDL
     QTEQESQKVM RRGPAAIAAY DSAGNPTPAL LGFAKSCGVT VDALTKTQTD KGEWIVFETQ
     SEGTKTKDLL PGLVSQSLES LPIAKPMRWG EGDDEFARPV HWAVMLYGSE TLNHKILGVT
     SGCHSRGHRF HHPQEIRINS AASYEDQMKD AFVIADFATR RQAIIHQVQE LAAPLGASVV
     MPEELVDEVT SIVEWPQALI ANFEQEFLEV PAEALIASMQ SHQKCFALKN KHGELLPYFI
     TVSNIASSNP KQVVLGNEKV MRARLSDAAF FFKQDKKQPL SAHIPSTEQV IFQVKLGSVY
     DKVQRIKVMM DHLSQSLNLP SHLAERATLL SKCDLMTGMV GEFPELQGIM GYYYALNDGE
     EAVVATALNE QYMPRFSGDD LPSTDLGKAL SLVDRMDTLV GIFAIGQKPT GVKDPFKLRR
     HALAVVRLLI SISAPLNLST LIKEALANYG DRLPQDKNLV AELKPFILER LQSYYQNQGI
     SADLVHAVRA RQDDWLYDLD KRLFALKSFI TMPEATSLSA ACKRVGNILA QAAYADKKVD
     IKEELIEEGA EKALFDHLNK ITKTVETLYI AGDYQALLKL LASLKEPVDA FFDHVMVMVE
     EESLKQNRLA LLQRLQELLQ GVADISML
//
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