SYM_BRUSU
ID SYM_BRUSU Reviewed; 515 AA.
AC P59078; G0K9R9;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
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};
GN OrderedLocusNames=BR0995, BS1330_I0991;
OS Brucella suis biovar 1 (strain 1330).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=204722;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=12271122; DOI=10.1073/pnas.192319099;
RA Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT "The Brucella suis genome reveals fundamental similarities between animal
RT and plant pathogens and symbionts.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1330;
RX PubMed=22038969; DOI=10.1128/jb.06181-11;
RA Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT "Revised genome sequence of Brucella suis 1330.";
RL J. Bacteriol. 193:6410-6410(2011).
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: Monomer. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE014291; AAN29918.1; -; Genomic_DNA.
DR EMBL; CP002997; AEM18335.1; -; Genomic_DNA.
DR RefSeq; WP_004689678.1; NZ_KN046804.1.
DR PDB; 5K0S; X-ray; 2.45 A; A/B/C=1-515.
DR PDB; 5K0T; X-ray; 2.60 A; A/B/C=1-515.
DR PDBsum; 5K0S; -.
DR PDBsum; 5K0T; -.
DR AlphaFoldDB; P59078; -.
DR SMR; P59078; -.
DR EnsemblBacteria; AEM18335; AEM18335; BS1330_I0991.
DR GeneID; 45052047; -.
DR KEGG; bms:BR0995; -.
DR KEGG; bsi:BS1330_I0991; -.
DR PATRIC; fig|204722.21.peg.732; -.
DR HOGENOM; CLU_009710_9_4_5; -.
DR OMA; SDMHGTP; -.
DR PhylomeDB; P59078; -.
DR Proteomes; UP000007104; Chromosome I.
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:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 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; 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; IPR014729; Rossmann-like_a/b/a_fold.
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 PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; SSF47323; 1.
DR TIGRFAMs; TIGR00398; metG; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..515
FT /note="Methionine--tRNA ligase"
FT /id="PRO_0000139213"
FT MOTIF 13..23
FT /note="'HIGH' region"
FT MOTIF 300..304
FT /note="'KMSKS' region"
FT BINDING 303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01228"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 21..39
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 55..64
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 68..85
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 91..95
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 99..114
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 118..122
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 125..128
FT /evidence="ECO:0007829|PDB:5K0S"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 172..181
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 189..200
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 229..234
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 236..239
FT /evidence="ECO:0007829|PDB:5K0S"
FT TURN 240..244
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 249..253
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 257..262
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 266..270
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 272..279
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 311..318
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 320..330
FT /evidence="ECO:0007829|PDB:5K0S"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 341..351
FT /evidence="ECO:0007829|PDB:5K0S"
FT TURN 352..355
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 383..404
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 408..429
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 431..437
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 439..460
FT /evidence="ECO:0007829|PDB:5K0S"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 465..474
FT /evidence="ECO:0007829|PDB:5K0S"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:5K0T"
FT HELIX 486..489
FT /evidence="ECO:0007829|PDB:5K0S"
SQ SEQUENCE 515 AA; 57998 MW; B3CBD8FA93515199 CRC64;
MSREKYYITT AIAYPNGKPH IGHAYELIAT DAMARFQRLN GMDVYFLTGT DEHGIKMLQS
ARKEGITPRE LADRNTSAFR RMAEVLNSSN DDYIRTSEER HYKASQAIWQ AMVANGDIYK
GGYAGWYSVR DEAYYGEEET EVRADGVRYG PQGTPVEWVE EESYFFRLSA YQDKLLDLYE
NNPGFIMPAE RRNEIVSFVK SGLKDLSISR TTFDWGIPVP GDEKHVMYVW VDALTNYITA
LGYPDTTDER WAYWPANAHI IGKDISRFHA VYWPAFLMSA QLPLPKRVFA HGFLFNRGEK
MSKSVGNVID PFELVERYGL DQLRYFLMRE VPFGQDGSYS HEAIVNRTNA DLANDLGNLA
QRSLSMIAKN CEGKVPQPGA FSEADKAILD QADAALETAR KAMDDQALHL ALGAIFAVVA
EANRYFAGQE PWALRKTDPA RMGTVLYVTA EVLRRVGIMV QPFIPQSAEK LLDILAVPAD
KRQFADVLAS PLAGGTDLPA PQPVFPRYVE ADEQN
