ID Q65PI3_BACLD Unreviewed; 662 AA.
AC Q65PI3; Q62ZX2;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 154.
DE RecName: Full=Methionine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_01228};
DE EC=6.1.1.10 {ECO:0000256|HAMAP-Rule:MF_01228};
DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_01228};
DE Short=MetRS {ECO:0000256|HAMAP-Rule:MF_01228};
GN Name=metS {ECO:0000313|EMBL:AAU21686.1};
GN Synonyms=metG {ECO:0000256|HAMAP-Rule:MF_01228};
GN OrderedLocusNames=BL00533 {ECO:0000313|EMBL:AAU21686.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU21686.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU21686.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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:0000256|ARBA:ARBA00003314,
CC ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00001234, ECO:0000256|HAMAP-
CC Rule:MF_01228};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_01228}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01228}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC MetG type 2B subfamily. {ECO:0000256|HAMAP-Rule:MF_01228}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01228}.
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DR EMBL; CP000002; AAU21686.1; -; Genomic_DNA.
DR RefSeq; WP_003178175.1; NC_006322.1.
DR AlphaFoldDB; Q65PI3; -.
DR STRING; 279010.BL00533; -.
DR GeneID; 66213657; -.
DR KEGG; bli:BL00533; -.
DR PATRIC; fig|279010.13.peg.42; -.
DR eggNOG; COG0073; Bacteria.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_4_9; -.
DR Proteomes; UP000000606; 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-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 CDD; cd02800; tRNA_bind_EcMetRS_like; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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 NCBIfam; TIGR00398; metG; 1.
DR NCBIfam; TIGR00399; metG_C_term; 1.
DR PANTHER; PTHR43326:SF1; METHIONINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43326; METHIONYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
DR PROSITE; PS50886; TRBD; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000256|HAMAP-Rule:MF_01228};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01228};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01228};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_01228}; Reference proteome {ECO:0000313|Proteomes:UP000000606};
KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_01228};
KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW Rule:MF_01228}.
FT DOMAIN 562..662
FT /note="TRNA-binding"
FT /evidence="ECO:0000259|PROSITE:PS50886"
FT MOTIF 15..25
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 311..315
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ SEQUENCE 662 AA; 75794 MW; 6B36EB2F56133F8E CRC64;
MPQEKNTFYI TTPIYYPSGK LHIGHAYTTV AGDAMARYKR LRGFDVRYLT GTDEHGQKIQ
QTAEKENITP QELVDRAAED IQQLWKKLDI SNDDFIRTTE ERHKKVIEKV FQKLLDNGDI
YLDEYEGWYS IPDETFYTET QLVDVERNEK GEVIGGKSPD SGHPVELIKE ESYFFRMGKY
ADRLLAFYEE NPEFIQPESR KNEMINNFIK PGLEDLAVSR TTFDWGIKVP GNPKHVIYVW
IDALFNYITA LGFNTENDEN YQKYWPADVH LVGKEIVRFH TIYWPIMLMA LDLPLPKKVF
AHGWLLMKDG KMSKSKGNVV DPVTLIDRYG LDALRYYLLR EVPFGSDGVF TPEGFVERIN
YDLANDLGNL LNRTVAMVNK YFDGRIQSYE GPVTAFDEPL SSFSQKTIEA YEQAIENMEF
SVALSSLWQF VSRTNKYIDE TAPWVLAKDK DKEKELQSVM YHLAESLRIT AVLLQPFLTQ
TPEKIFAQLG VTDASLKTWD SIQSFGQLKS VTVQKGEPLF PRLEAEDEVA YIKSKMQGTA
PKEEPKQEEK AHERLPEITI DDFMSTELRV AEVIHAEPVK KADRLLKLQL DLGFEKRQVV
SGIAKHYKPE ELVGRKVICV TNLKPVKLRG ELSQGMILAG EDNGVLSLAA VDSSLANGTR
IK
//
