(data stored in ACNUC7421 zone)

SWISSPROT: SYM_BACSU

ID   SYM_BACSU               Reviewed;         664 AA.
AC   P37465;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   11-DEC-2019, entry version 145.
DE   RecName: Full=Methionine--tRNA ligase;
DE            EC=6.1.1.10;
DE   AltName: Full=Methionyl-tRNA synthetase;
DE            Short=MetRS;
GN   Name=metG; Synonyms=metS; OrderedLocusNames=BSU00380;
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;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
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).
CC   -!- FUNCTION: Is required not only for elongation of protein synthesis but
CC       also for the initiation of all mRNA translation through initiator
CC       tRNA(fMet) aminoacylation. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-
CC         methionyl-tRNA(Met); Xref=Rhea:RHEA:13481, Rhea:RHEA-COMP:9667,
CC         Rhea:RHEA-COMP:9698, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:78442, ChEBI:CHEBI:78530,
CC         ChEBI:CHEBI:456215; EC=6.1.1.10;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       MetG type 2B subfamily. {ECO:0000305}.
DR   EMBL; D26185; BAA05273.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB11814.1; -; Genomic_DNA.
DR   PIR; S66067; S66067.
DR   RefSeq; NP_387919.1; NC_000964.3.
DR   RefSeq; WP_003226758.1; NZ_JNCM01000028.1.
DR   SMR; P37465; -.
DR   IntAct; P37465; 3.
DR   MINT; P37465; -.
DR   STRING; 224308.BSU00380; -.
DR   jPOST; P37465; -.
DR   PaxDb; P37465; -.
DR   PRIDE; P37465; -.
DR   EnsemblBacteria; CAB11814; CAB11814; BSU00380.
DR   GeneID; 936877; -.
DR   KEGG; bsu:BSU00380; -.
DR   PATRIC; fig|224308.179.peg.38; -.
DR   eggNOG; ENOG4105CKH; Bacteria.
DR   eggNOG; COG0073; LUCA.
DR   eggNOG; COG0143; LUCA.
DR   HOGENOM; HOG000200401; -.
DR   InParanoid; P37465; -.
DR   KO; K01874; -.
DR   OMA; SDMHGTP; -.
DR   PhylomeDB; P37465; -.
DR   BioCyc; BSUB:BSU00380-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004825; F:methionine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006431; P:methionyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd07957; Anticodon_Ia_Met; 1.
DR   CDD; cd00814; MetRS_core; 1.
DR   CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_01228; Met_tRNA_synth_type2; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR041872; Anticodon_Met.
DR   InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR   InterPro; IPR004495; Met-tRNA-synth_bsu_C.
DR   InterPro; IPR014758; Met-tRNA_synth.
DR   InterPro; IPR023457; Met-tRNA_synth_2.
DR   InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR   InterPro; IPR033911; MetRS_core.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR002547; tRNA-bd_dom.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 1.
DR   Pfam; PF01588; tRNA_bind; 1.
DR   PRINTS; PR01041; TRNASYNTHMET.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00398; metG; 1.
DR   TIGRFAMs; TIGR00399; metG_C_term; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR   PROSITE; PS50886; TRBD; 1.
PE   3: Inferred from homology;
DR   PRODOM; P37465.
DR   SWISS-2DPAGE; P37465.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW   tRNA-binding.
FT   CHAIN           1..664
FT                   /note="Methionine--tRNA ligase"
FT                   /id="PRO_0000139211"
FT   DOMAIN          570..662
FT                   /note="tRNA-binding"
FT   MOTIF           15..25
FT                   /note="'HIGH' region"
FT   MOTIF           311..315
FT                   /note="'KMSKS' region"
FT   BINDING         314
FT                   /note="ATP"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   664 AA;  76188 MW;  FF4C0575169E82DE CRC64;
     MPQENNTFYI TTPIYYPSGK LHIGHAYTTV AGDAMARYKR LKGFDVRYLT GTDEHGQKIQ
     QKAEQENITP QEYVDRAAAD IQKLWKQLEI SNDDFIRTTE KRHKVVIEKV FQKLLDNGDI
     YLDEYEGWYS IPDETFYTET QLVDIERNEK GEVIGGKSPD SGHPVELIKE ESYFFRMGKY
     ADRLLKYYEE NPTFIQPESR KNEMINNFIK PGLEDLAVSR TTFDWGVKVP ENPKHVVYVW
     IDALFNYLTA LGYDTENDEL YQKYWPADVH LVGKEIVRFH TIYWPIMLMA LDLPLPKQVF
     AHGWLLMKDG KMSKSKGNVV DPVTLIERYG LDELRYYLLR EVPFGSDGVF TPEGFVERIN
     YDLANDLGNL LNRTVAMINK YFDGQIGSYK GAVTEFDHTL TSVAEETVKA YEKAMENMEF
     SVALSTLWQL ISRTNKYIDE TAPWVLAKDP AKEEELRSVM YHLAESLRIS AVLLQPFLTK
     TPEKMFEQLG ITDESLKAWD SITAFGQLKD TKVQKGEPLF PRLEAEEEIA YIKGKMQGSA
     PAKEETKEEE PQEVDRLPEI TIDQFMDVEL RVAEVIEAEP VKKADRLLKL QLDLGFEKRQ
     VVSGIAKHYT PEELVGKKLV CVTNLKPVKL RGELSQGMIL AGEADGVLKV VSIDQSLPKG
     TRIK
//

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