SYM_STAS1
ID SYM_STAS1 Reviewed; 658 AA.
AC Q49UZ9;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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}; OrderedLocusNames=SSP2266;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE19411.1; -; Genomic_DNA.
DR RefSeq; WP_011303878.1; NZ_MTGA01000029.1.
DR AlphaFoldDB; Q49UZ9; -.
DR SMR; Q49UZ9; -.
DR STRING; 342451.SSP2266; -.
DR EnsemblBacteria; BAE19411; BAE19411; SSP2266.
DR KEGG; ssp:SSP2266; -.
DR PATRIC; fig|342451.11.peg.2257; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_9; -.
DR OMA; SDMHGTP; -.
DR OrthoDB; 761140at2; -.
DR Proteomes; UP000006371; 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; 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; PF19303; Anticodon_3; 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;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding.
FT CHAIN 1..658
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139248"
FT DOMAIN 558..658
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 658 AA; 75165 MW; E44A9B7A9DBAD6B0 CRC64;
MAKETFYITT PIYYPSGNLH IGHAYTTTAG DVIARYKRMQ GYDVRYLTGT DEHGQKIQEK
AQKAGKSEIE YLDEMIAGIK DLWGKLEISN DDFIRTTEIR HKEVVQQIFE RLLAQGDIYL
GEYEGWYSVP DETYYTETQL VDPIMENGVI VGGKSPDSGH EVELVKEESY FFNLSKYTDR
LLEFYDENPE FIQPPSRKNE MINNFIKPGL EDLAVSRTSF DWGIRVQSNP KHVVYVWIDA
LVNYISSLGY LSDDDSLFKK YWPADIHIMA KEIVRFHSII WPILLMALDI PLPKKVFAHG
WILMKDGKMS KSKGNVVDPN VLINRYGLDA TRYYLMRELP FGSDGVFTPE GFVERTNYDL
ANDLGNLVNR TISMVNKYFD GELPAYQGPK HELDKDMEQM ALDTVKTFHE NMDDLQFSVA
LSTIWKFISR TNKYIDETSP WVLAKDEDQK EMLGNVMAHL VENIRIIAVL LRPFLTHAPK
QIFSQLNINA PELFELESIE QYGALTEPIM VSGKPEPIFP RLDSEVEISY IKESMQPDKI
EEEVEEELPS KAQIDIKDFD KVEIKAATII DAEQVKKSDK LLKIQVDLDS EQRQIVSGIA
KFYQPEDIIG KKVAVVTNLK PAKLMGRKSE GMILSAEKDG VLTLVSLPSA IPNGAIIK
