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Reviewed, UniProtKB/Swiss-Prot Q65JJ1 (SYP_BACLD)

Last modified February 9, 2010. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Prolyl-tRNA synthetase
    EC=6.1.1.15
Alternative name(s):
    Proline--tRNA ligase
      Short name=ProRS
Gene names
Name: proS
Ordered Locus Names: BLi01878, BL01235
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Catalyzes the attachment of proline to tRNA(Pro) in a two-step reaction: proline is first activated by ATP to form Pro-AMP and then transferred to the acceptor end of tRNA(Pro). As ProRS can inadvertently accommodate and process non-cognate amino acids such as alanine and cysteine, to avoid such errors it has two additional distinct editing activities against alanine. One activity is designated as 'pretransfer' editing and involves the tRNA(Pro)-independent hydrolysis of activated Ala-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Ala-tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS By similarity. HAMAP MF_01569

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP MF_01569

Subunit structure

Homodimer By similarity. HAMAP MF_01569

Subcellular location

Cytoplasm By similarity HAMAP MF_01569.

Domain

Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain By similarity. HAMAP MF_01569

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

proline-tRNA ligase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Prolyl-tRNA synthetase HAMAP MF_01569
PRO_0000248648

Sequences

Sequence LengthMass (Da)Tools
Q65JJ1-1 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 5F38EB6AC80A6ECD

FASTA57264,138
        10         20         30         40         50         60 
MRQSRTLIPT LREVPADAEA KSHQLLLRAG FIRQNTSGVY SYMPLANKVI HKIQSIVREE 

        70         80         90        100        110        120 
MEKINAVEML MPALQQAETW QESGRWYTYG PELMRLKDRH GREFALGATH EEVITSIVRD 

       130        140        150        160        170        180 
EVKSYKRLPL TLYQIQSKFR DEKRPRFGLL RGREFIMKDA YSFHSSAESL DETYNDMYQA 

       190        200        210        220        230        240 
YTNVFTRCGL NFRPVIADSG AMGGKDTHEF MALSDVGEDT IAYSDQSSYA ANIEMAEVKE 

       250        260        270        280        290        300 
TDAGEQAEMK ELQEVHTPSV KTIEEVAAFL GISPSDCIKS MLMKADGRFV LVLTRGDHEV 

       310        320        330        340        350        360 
NDVKVKNLLQ AEIIEFASAE EVAEITGTEP GFVGPVGLDR EIEIFADFAV KAMANAAAGA 

       370        380        390        400        410        420 
NKTDYHYQNV NISRDAHNVT FADLRFIQEG DPSPDGKGTI RFAKGIEVGQ VFKLGTRYSE 

       430        440        450        460        470        480 
AMDATYLDEN GRAQPMLMGC YGIGISRTLS AIVEQHHDDK GLIWPLEVTP YDLHILALNM 

       490        500        510        520        530        540 
KNDAQVQLAE KLYEEFKANG YDVLFDDRAE RAGVKFADSD LIGLPIRITV GKRADEGVVE 

       550        560        570 
VKIRKTGESF EIAADELFDF IEKQVKSLSS HS 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed: 15383718] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed: 15461803] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU40773.1.
CP000002 Genomic DNA. Translation: AAU23413.1.
RefSeqYP_079051.1.
YP_091466.1.

3D structure databases

SMRQ65JJ1. Positions 1-563.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ65JJ1.

Genome annotation databases

GeneID3031073.
3101626.
GenomeReviewsGene locus BLi01878 in contig AE017333_GR.
Gene locus BL01235 in contig CP000002_GR.
KEGGbld:BLi01878.
bli:BL01235.
NMPDRfig|279010.5.peg.2582.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0442.
HOGENOMHBG403504.
OMADFVLGPT.

Enzyme and pathway databases

BioCycBLIC279010-1:BLI01878-MONOMER.
BLIC279010:BL01235-MONOMER.

Family and domain databases

HAMAPMF_01569. Pro_tRNA_synth_type1.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II_cons-dom.
IPR004154. Anticodon_bd.
IPR004500. Pro-tRNA-synth_IIa_bac.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
Gene3DG3DSA:3.40.50.800. Anticodon_bd. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSYP_BACLD
AccessionPrimary (citable) accession number: Q65JJ1
Secondary accession number(s): Q62UZ6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: October 25, 2004
Last modified: February 9, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents