ID SYM_ECO45 Reviewed; 677 AA.
AC B7MEG9;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 01-MAY-2013, entry version 36.
DE RecName: Full=Methionine--tRNA ligase;
DE EC=6.1.1.10;
DE AltName: Full=Methionyl-tRNA synthetase;
DE Short=MetRS;
GN Name=metG; OrderedLocusNames=ECS88_2256;
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A.,
RA Chiapello H., Clermont O., Cruveiller S., Danchin A., Diard M.,
RA Dossat C., Karoui M.E., Frapy E., Garry L., Ghigo J.M., Gilles A.M.,
RA Johnson J., Le Bouguenec C., Lescat M., Mangenot S.,
RA Martinez-Jehanne V., Matic I., Nassif X., Oztas S., Petit M.A.,
RA Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J., Vacherie B.,
RA Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- FUNCTION: Is required not only for elongation of protein synthesis
CC but also for the initiation of all mRNA translation through
CC initiator tRNA(fMet) aminoacylation (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP +
CC diphosphate + L-methionyl-tRNA(Met).
CC -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC family. MetG type 1 subfamily.
CC -!- SIMILARITY: Contains 1 tRNA-binding domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CU928161; CAR03542.1; -; Genomic_DNA.
DR RefSeq; YP_002391946.1; NC_011742.1.
DR ProteinModelPortal; B7MEG9; -.
DR SMR; B7MEG9; 5-551, 570-676.
DR STRING; 585035.ECS88_2256; -.
DR EnsemblBacteria; CAR03542; CAR03542; ECS88_2256.
DR GeneID; 7129612; -.
DR KEGG; ecz:ECS88_2256; -.
DR PATRIC; 18412224; VBIEscCol91599_2236.
DR eggNOG; COG0143; -.
DR HOGENOM; HOG000200400; -.
DR KO; K01874; -.
DR OMA; RMHGHEV; -.
DR ProtClustDB; PRK00133; -.
DR BioCyc; ECOL585035:GJWP-2253-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:HAMAP.
DR GO; GO:0000049; F:tRNA binding; IEA:HAMAP.
DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:HAMAP.
DR Gene3D; 2.40.50.140; -; 1.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1; -.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR004495; Met-tRNA-synth_Ia_bsu_C.
DR InterPro; IPR023458; Met-tRNA_ligase_1.
DR InterPro; IPR014758; Met-tRNA_synth.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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_1a_anticodon-bd.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR Pfam; PF01588; tRNA_bind; 1.
DR PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 1.
DR SUPFAM; SSF47323; tRNAsyn_1a_bind; 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; Complete proteome; Cytoplasm;
KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1 677 Methionine--tRNA ligase.
FT /FTId=PRO_1000199287.
FT DOMAIN 575 677 tRNA-binding.
FT MOTIF 15 25 "HIGH" region.
FT MOTIF 333 337 "KMSKS" region.
FT METAL 146 146 Zinc (By similarity).
FT METAL 149 149 Zinc (By similarity).
FT METAL 159 159 Zinc (By similarity).
FT METAL 162 162 Zinc (By similarity).
FT BINDING 336 336 ATP (By similarity).
SQ SEQUENCE 677 AA; 76284 MW; 3528021F3AD9600B CRC64;
MTQVAKKILV TCALPYANGS IHLGHMLEHI QADVWVRYQR MRGHEVNFIC ADDAHGTPIM
LKAQQLGITP EQMIGEMSQE HQTDFAGFNI SYDNYHSTHS EENRQLSELI YSRLKENGFI
KNRTISQLYD PEKGMFLPDR FVKGTCPKCK SPDQYGDNCE VCGATYSPTE LIEPKSVVSG
ATPVMRDSEH FFFDLPSFSE MLQAWTRSGA LQEQVANKMQ EWFESGLQQW DISRDAPYFG
FEIPNAPGKY FYVWLDAPIG YMGSFKNLCD KRGDSVSFDK YWKKDSTAEL YHFIGKDIVY
FHSLFWPAML EGSNFRKPTN LFVHGYVTVN GAKMSKSRGT FIKASTWLNH FDADSLRYYY
TAKLSSRIDD IDLNLEDFVQ RVNADIVNKV VNLASRNAGF INKRFDGVLA SELADPQLYK
TFTDAAEVIG EAWESREFGK AIREIMALAD LANRYVDEQA PWVVAKQEGR DADLQAICSM
GINLFRVLMT YLKPVLPKLT ERAEAFLNTE LTWDGIQQPL LGHKVNPFKA LYNRIDMKQV
EALVEASKEE VKATAAPVTG PLADDPIQET ITFDDFAKVD LRVALIENAE FVEGSDKLLR
LTLDLGGEKR NVFSGIRSAY PDPQALIGRH TIMVANLAPR KMRFGISEGM VMAAGPGGKD
IFLLSPDAGA KPGHQVK
//
