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SYGB_BACSU
ID   SYGB_BACSU              Reviewed;         679 AA.
AC   P54381;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Glycine--tRNA ligase beta subunit;
DE            EC=6.1.1.14;
DE   AltName: Full=Glycyl-tRNA synthetase beta subunit;
DE            Short=GlyRS;
GN   Name=glyS; Synonyms=yqfK; OrderedLocusNames=BSU25260;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 481 AND 611.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-
CC         tRNA(Gly); Xref=Rhea:RHEA:16013, Rhea:RHEA-COMP:9664, Rhea:RHEA-
CC         COMP:9683, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522, ChEBI:CHEBI:456215;
CC         EC=6.1.1.14;
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000305}.
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DR   EMBL; D84432; BAA12485.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14455.2; -; Genomic_DNA.
DR   PIR; B69636; B69636.
DR   RefSeq; NP_390404.2; NC_000964.3.
DR   RefSeq; WP_003230059.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P54381; -.
DR   SMR; P54381; -.
DR   IntAct; P54381; 1.
DR   MINT; P54381; -.
DR   STRING; 224308.BSU25260; -.
DR   jPOST; P54381; -.
DR   PaxDb; P54381; -.
DR   PRIDE; P54381; -.
DR   EnsemblBacteria; CAB14455; CAB14455; BSU_25260.
DR   GeneID; 937887; -.
DR   KEGG; bsu:BSU25260; -.
DR   PATRIC; fig|224308.179.peg.2745; -.
DR   eggNOG; COG0751; Bacteria.
DR   InParanoid; P54381; -.
DR   OMA; LPIPKRM; -.
DR   PhylomeDB; P54381; -.
DR   BioCyc; BSUB:BSU25260-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004820; F:glycine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006426; P:glycyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00255; Gly_tRNA_synth_beta; 1.
DR   InterPro; IPR015944; Gly-tRNA-synth_bsu.
DR   InterPro; IPR006194; Gly-tRNA-synth_heterodimer.
DR   PANTHER; PTHR30075; PTHR30075; 1.
DR   Pfam; PF02092; tRNA_synt_2f; 1.
DR   PRINTS; PR01045; TRNASYNTHGB.
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; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..679
FT                   /note="Glycine--tRNA ligase beta subunit"
FT                   /id="PRO_0000072894"
FT   CONFLICT        481
FT                   /note="R -> P (in Ref. 1; BAA12485)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        611
FT                   /note="Q -> E (in Ref. 1; BAA12485)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   679 AA;  76291 MW;  52B230FDDF82D94F CRC64;
     MSKQDLLLEI GLEEMPARFL NESMVQLGDK LTGWLKEKNI THGEVKLFNT PRRLAVFVKD
     VAEKQDDIKE EAKGPAKKIA LDADGNWTKA AIGFSKGQGA NVEDLYIKEV KGIEYVFVQK
     FQAGQETKSL LPELSGLITS LHFPKNMRWG NEDLRYIRPI KWIVALFGQD VIPFSITNVE
     SGRTTQGHRF LGHEVSIESP SAYEEQLKGQ HVIADPSVRK QMIQSQLETM AAENNWSIPV
     DEDLLDEVNH LVEYPTALYG SFESEFLSIP EEVLVTTMKE HQRYFPVKDK NGDLLPHFIT
     VRNGNSHAIE NVARGNEKVL RARLSDASFF YKEDQKLNID ANVKKLENIV FHEELGSLAD
     KVRRVTSIAE KLAVRLQADE DTLKHVKRAA EISKFDLVTH MIYEFPELQG IMGEKYARML
     GEDEAVAAAV NEHYMPRSAG GETPSTFTGA VVAMADKLDT IASFFSIGVI PTGSQDPYGL
     RRQASGIVAI LLDRNWGISF EELLTFVQTD KENELLDFFT QRLKYVLNAE QIRHDVIDAV
     LESSELEPYS ALHKAQVLEQ KLGAPGFKET AEALGRVISI SKKGVRGDIQ PDLFENEYEA
     KLFDAYQTAK QNLQENFSKK DYEAALASLA ALKEPIDAYF DHTMVIADNE SLKANRLAQM
     VSLADEIKSF ANMNALIVK
 
 
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