SYM_STAAN
ID SYM_STAAN Reviewed; 657 AA.
AC P67579; Q99WB3;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01228};
DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_01228};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01228};
DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_01228};
GN Name=metG {ECO:0000255|HAMAP-Rule:MF_01228}; Synonyms=metS;
GN OrderedLocusNames=SA0448;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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:0000255|HAMAP-Rule:MF_01228}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01228};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01228}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2B subfamily. {ECO:0000255|HAMAP-Rule:MF_01228}.
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DR EMBL; BA000018; BAB41678.1; -; Genomic_DNA.
DR PIR; C89815; C89815.
DR RefSeq; WP_001051129.1; NC_002745.2.
DR AlphaFoldDB; P67579; -.
DR SMR; P67579; -.
DR EnsemblBacteria; BAB41678; BAB41678; BAB41678.
DR KEGG; sau:SA0448; -.
DR HOGENOM; CLU_009710_9_4_9; -.
DR OMA; SDMHGTP; -.
DR Proteomes; UP000000751; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 2.40.50.140; -; 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 PANTHER; PTHR43326; PTHR43326; 1.
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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding.
FT CHAIN 1..657
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139241"
FT DOMAIN 557..657
FT /note="tRNA-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT MOTIF 13..23
FT /note="'HIGH' region"
FT MOTIF 308..312
FT /note="'KMSKS' region"
FT BINDING 311
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
SQ SEQUENCE 657 AA; 74873 MW; 48C3CE9FE519D017 CRC64;
MAKETFYITT PIYYPSGNLH IGHAYSTVAG DVIARYKRMQ GYDVRYLTGT DEHGQKIQEK
AQKAGKTEIE YLDEMIAGIK QLWAKLEISN DDFIRTTEER HKHVVEQVFE RLLKQGDIYL
GEYEGWYSVP DETYYTESQL VDPQYENGKI IGGKSPDSGH EVELVKEESY FFNISKYTDR
LLEFYDQNPD FIQPPSRKNE MINNFIKPGL ADLAVSRTSF NWGVHVPSNP KHVVYVWIDA
LVNYISALGY LSDDESLFNK YWPADIHLMA KEIVRFHSII WPILLMALDL PLPKKVFAHG
WILMKDGKMS KSKGNVVDPN ILIDRYGLDA TRYYLMRELP FGSDGVFTPE AFVERTNFDL
ANDLGNLVNR TISMVNKYFD GELPAYQGPL HELDEEMEAM ALETVKSYTE SMESLQFSVA
LSTVWKFISR TNKYIDETTP WVLAKDDSQK DMLGNVMAHL VENIRYAAVL LRPFLTHAPK
EIFEQLNINN PQFMEFSSLE QYGVLTESIM VTGQPKPIFP RLDSEAEIAY IKESMQPPAT
EEEKEEIPSK PQIDIKDFDK VEIKAATIID AEHVKKSDKL LKIQVDLDSE QRQIVSGIAK
FYTPDDIIGK KVAVVTNLKP AKLMGQKSEG MILSAEKDGV LTLVSLPSAI PNGAVIK
