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P37465 (SYM_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Methionine--tRNA ligase
EC=6.1.1.10
Alternative name(s):
Methionyl-tRNA synthetase
Short name=MetRS
Gene names
Name:metG
Synonyms:metS
Ordered Locus Names:BSU00380
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length664 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation By similarity. HAMAP MF_01228

Catalytic activity

ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met). HAMAP MF_01228

Subunit structure

Homodimer By similarity. HAMAP MF_01228

Subcellular location

Cytoplasm HAMAP MF_01228.

Sequence similarities

Belongs to the class-I aminoacyl-tRNA synthetase family. MetG type 2B subfamily.

Contains 1 tRNA-binding domain.

Ontologies

Keywords
   Biological processProtein biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionAminoacyl-tRNA synthetase
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processmethionyl-tRNA aminoacylation

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

methionine-tRNA ligase activity

Inferred from electronic annotation. Source: EC

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 664664Methionine--tRNA ligase HAMAP MF_01228
PRO_0000139211

Regions

Domain570 – 66293tRNA-binding
Motif15 – 2511"HIGH" region HAMAP MF_01228
Motif311 – 3155"KMSKS" region HAMAP MF_01228

Sites

Binding site3141ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P37465 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: FF4C0575169E82DE

FASTA66476,188
        10         20         30         40         50         60 
MPQENNTFYI TTPIYYPSGK LHIGHAYTTV AGDAMARYKR LKGFDVRYLT GTDEHGQKIQ 

        70         80         90        100        110        120 
QKAEQENITP QEYVDRAAAD IQKLWKQLEI SNDDFIRTTE KRHKVVIEKV FQKLLDNGDI 

       130        140        150        160        170        180 
YLDEYEGWYS IPDETFYTET QLVDIERNEK GEVIGGKSPD SGHPVELIKE ESYFFRMGKY 

       190        200        210        220        230        240 
ADRLLKYYEE NPTFIQPESR KNEMINNFIK PGLEDLAVSR TTFDWGVKVP ENPKHVVYVW 

       250        260        270        280        290        300 
IDALFNYLTA LGYDTENDEL YQKYWPADVH LVGKEIVRFH TIYWPIMLMA LDLPLPKQVF 

       310        320        330        340        350        360 
AHGWLLMKDG KMSKSKGNVV DPVTLIERYG LDELRYYLLR EVPFGSDGVF TPEGFVERIN 

       370        380        390        400        410        420 
YDLANDLGNL LNRTVAMINK YFDGQIGSYK GAVTEFDHTL TSVAEETVKA YEKAMENMEF 

       430        440        450        460        470        480 
SVALSTLWQL ISRTNKYIDE TAPWVLAKDP AKEEELRSVM YHLAESLRIS AVLLQPFLTK 

       490        500        510        520        530        540 
TPEKMFEQLG ITDESLKAWD SITAFGQLKD TKVQKGEPLF PRLEAEEEIA YIKGKMQGSA 

       550        560        570        580        590        600 
PAKEETKEEE PQEVDRLPEI TIDQFMDVEL RVAEVIEAEP VKKADRLLKL QLDLGFEKRQ 

       610        620        630        640        650        660 
VVSGIAKHYT PEELVGKKLV CVTNLKPVKL RGELSQGMIL AGEADGVLKV VSIDQSLPKG 


TRIK

« Hide

References

« Hide 'large scale' references
[1]"Systematic sequencing of the 180 kilobase region of the Bacillus subtilis chromosome containing the replication origin."
Ogasawara N., Nakai S., Yoshikawa H.
DNA Res. 1:1-14(1994) [PubMed: 7584024] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		D26185 Genomic DNA. Translation: BAA05273.1.
AL009126 Genomic DNA. Translation: CAB11814.1.
PIRS66067.
RefSeqNP_387919.1. NC_000964.3.

3D structure databases

ProteinModelPortalP37465.
SMRP37465. Positions 5-663.
ModBaseSearch...

Protein-protein interaction databases

IntActP37465. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000003089; EBBACP00000003089; EBBACG00000003083.
GeneID936877.
GenomeReviewsGene locus BSU00380 in contig AL009126_GR.
KEGGbsu:BSU00380.
NMPDRfig|224308.1.peg.38.
PATRIC18971547. VBIBacSub10457_0039.

Organism-specific databases

GenoListBSU00380. [Micado]

Phylogenomic databases

GeneTreeEBGT00070000031891.
HOGENOMHBG721667.
OMAFDWGIKV.
PhylomeDBP37465.
ProtClustDBPRK12267.

Enzyme and pathway databases

BioCycBSUB:BSU00380-MONOMER.

Family and domain databases

HAMAPMF_01228. Met_tRNA_synth_type2. Fused.
[Tree]
InterProIPR015413. aa-tRNA-synt_I.
IPR001412. aa-tRNA-synth_I_CS.
IPR004495. Met-tRNA-synth_Ia_bsu_C.
IPR014758. Met-tRNA_synth.
IPR023457. Met-tRNA_synth_2.
IPR012340. NA-bd_OB-fold.
IPR016027. NA-bd_OB-fold-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR002547. tRNA-bd_dom.
IPR009080. tRNAsynth_1a_anticodon-bd.
IPR013155. V/L/I-tRNA-synth_anticodon-bd.
[Graphical view]
Gene3DG3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 2 hits.
KOK01874.
PfamPF08264. Anticodon_1. 1 hit.
PF09334. tRNA-synt_1g. 1 hit.
PF01588. tRNA_bind. 1 hit.
[Graphical view]
PRINTSPR01041. TRNASYNTHMET.
SUPFAMSSF50249. Nucleic_acid_OB. 1 hit.
SSF47323. tRNAsyn_1a_bind. 1 hit.
TIGRFAMsTIGR00398. MetG. 1 hit.
TIGR00399. MetG_C_term. 1 hit.
PROSITEPS00178. AA_TRNA_LIGASE_I. 1 hit.
PS50886. TRBD. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYM_BACSU
AccessionPrimary (citable) accession number: P37465
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: January 25, 2012
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents