ID C6ADT7_BARGA Unreviewed; 519 AA.
AC C6ADT7;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 96.
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:ACS51342.1};
GN Synonyms=metG {ECO:0000256|HAMAP-Rule:MF_01228};
GN OrderedLocusNames=Bgr_10810 {ECO:0000313|EMBL:ACS51342.1};
OS Bartonella grahamii (strain as4aup).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=634504 {ECO:0000313|EMBL:ACS51342.1, ECO:0000313|Proteomes:UP000001489};
RN [1] {ECO:0000313|EMBL:ACS51342.1, ECO:0000313|Proteomes:UP000001489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=as4aup {ECO:0000313|Proteomes:UP000001489};
RX PubMed=19578403; DOI=10.1371/journal.pgen.1000546;
RA Berglund E.C., Frank A.C., Calteau A., Vinnere Pettersson O., Granberg F.,
RA Eriksson A.-S., Naeslund K., Holmberg M., Lindroos H., Andersson S.G.;
RT "Run-off replication of host-adaptability genes is associated with gene
RT transfer agents in the genome of mouse-infecting Bartonella grahamii.";
RL PLoS Genet. 5:E1000546-E1000546(2009).
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01228};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-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; CP001562; ACS51342.1; -; Genomic_DNA.
DR RefSeq; WP_015856397.1; NC_012846.1.
DR AlphaFoldDB; C6ADT7; -.
DR STRING; 634504.Bgr_10810; -.
DR KEGG; bgr:Bgr_10810; -.
DR eggNOG; COG0143; Bacteria.
DR HOGENOM; CLU_009710_9_3_5; -.
DR OrthoDB; 9810191at2; -.
DR Proteomes; UP000001489; 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:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd07957; Anticodon_Ia_Met; 1.
DR CDD; cd00814; MetRS_core; 1.
DR Gene3D; 2.170.220.10; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00398; metG; 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 PRINTS; PR01041; TRNASYNTHMET.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 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}.
FT DOMAIN 5..364
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 375..507
FT /note="Methionyl-tRNA synthetase anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF19303"
FT MOTIF 12..22
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
FT MOTIF 300..304
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01228"
SQ SEQUENCE 519 AA; 59681 MW; 4FEE732D21BB463E CRC64;
MRDTYYITTP IFYPNGAPHI GHAYSAIASD VLARFQRLNG KNVFFLSGTD EHGLKMQQTA
AALGMTPQQL ADRNSAVFQK MLAVLNCSND DFIRTTEERH YQACQEIWKK MEANGDIYLG
RYTGWYSVRQ EAYYEEKDTE IGPDNIRREK ELGSPVEWNE EESYFFRLSH YEKALLEYYE
KHPDFIAPLE RRNEIISFIK SGLKDISISR ASFNWGIAVP ENPKHVMYVW VDALTNYLSA
IGFFNENSKK RDFWPANTHI IGKDIIRFHA VYWPAFLMSA GIELPKNIFA HGFLLNRGAK
MSKSIGNVVD PFEMVDHYGL DQVRYFLLRE VPFGQDGSYS HESLVNRINA DLANDLGNLA
QRCLSMIAKN CNAQVPRPTS FLAQDKQLLE QSLQVLETVH QAMSSYSMHL ALSAIFSIVA
DANRYFANEQ PWSLRKNDQE RFSTVLYITV EILRRIGIML LPFIPQSAAK LLDSLAVAED
DRLLYHISHS KIQEGLDLPP PEPIFPRYIL KKEDTYHVD
//
