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F0PQK2 (F0PQK2_BACT0) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Proline--tRNA ligase HAMAP-Rule MF_01569
EC=6.1.1.15 HAMAP-Rule MF_01569
Alternative name(s):
Prolyl-tRNA synthetase HAMAP-Rule MF_01569
Gene names
Name:proS HAMAP-Rule MF_01569
Ordered Locus Names:YBT020_18740 EMBL ADY22976.1
OrganismBacillus thuringiensis subsp. finitimus (strain YBT-020) [Complete proteome] [HAMAP]
Taxonomic identifier930170 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length566 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-Rule MF_01569 SAAS SAAS023717

Catalytic activity

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01569 SAAS SAAS023717

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01569 SAAS SAAS023717

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01569 SAAS SAAS023717.

Domain

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

Sequence similarities

Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily. HAMAP-Rule MF_01569

Sequences

Sequence LengthMass (Da)Tools
F0PQK2 [UniParc].

Last modified May 3, 2011. Version 1.
Checksum: 16D1F26FF6452B02

FASTA56663,122
        10         20         30         40         50         60 
MKQSMVFSPT LREVPADAEI KSHQLLLRAG FMRQNASGIY SFLPFGLKVL HKVERIVREE 

        70         80         90        100        110        120 
MERAGAVELL MPAMQAAELW QESGRWYSYG SELMRMKDRN AREFALGATH EEVITDLVRD 

       130        140        150        160        170        180 
EVKSYKKLPL TLYQIQTKFR DEQRPRFGLL RGREFLMKDA YSFHATQESL DEVYDRLYKA 

       190        200        210        220        230        240 
YSNIFARCGL NFRAVIADSG AMGGKDTHEF MVLSDVGEDT IAYSDTSDYA ANIEMAPVVA 

       250        260        270        280        290        300 
TYTKSDEAEK ALEKVATPDQ KAIEEVSAFL NIEAEKCIKS MVFKVDEKLV VVLVRGDHEV 

       310        320        330        340        350        360 
NDVKVKNVYG ASVVELASHE EVKELLNCEV GSLGPIGVTG DIEIIADHAV ASIVNGCSGA 

       370        380        390        400        410        420 
NEEGFHYVNV NPERDFKVSQ YTDLRFIQEG DQSPDGNGTI LFARGIEVGH VFKLGTRYSE 

       430        440        450        460        470        480 
AMNATFLDEN GKTQPLIMGC YGIGVSRTVA AIAEQFNDEN GLVWPKAVAP FHVHVIPVNM 

       490        500        510        520        530        540 
KSDAQREMGE NIYNSLQEQG YEVLLDDRAE RAGVKFADAD LFGLPVRVTV GKKADEGIVE 

       550        560 
VKVRATGESE EVKVEELQTY IANILK

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References

[1]"Complete genome sequence of Bacillus thuringiensis serovar finitimus strain YBT-020."
Zhu Y., Shang H., Zhu Q., Ji F., Wang P., Fu J., Deng Y., Xu C., Ye W., Zheng J., Zhu L., Ruan L., Peng D., Sun M.
J. Bacteriol. 193:2379-2380(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: YBT-020 EMBL ADY22976.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP002508 Genomic DNA. Translation: ADY22976.1.
RefSeqYP_005567394.1. NC_017200.1.

3D structure databases

ProteinModelPortalF0PQK2.
SMRF0PQK2. Positions 1-565.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADY22976; ADY22976; YBT020_18740.
GeneID12184774.
KEGGbtf:YBT020_18740.
PATRIC47093216. VBIBacThu177620_3724.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK01881.

Family and domain databases

Gene3D3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPMF_01569. Pro_tRNA_synth_type1.
InterProIPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR002316. Pro-tRNA-ligase_IIa.
IPR004500. Pro-tRNA-synth_IIa_bac-type.
IPR023717. Pro-tRNA-Synthase_IIa_type1.
IPR007214. YbaK/aa-tRNA-synth-assoc-dom.
[Graphical view]
PANTHERPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. YbaK. 1 hit.
[Graphical view]
PRINTSPR01046. TRNASYNTHPRO.
SUPFAMSSF52954. Anticodon_bd. 1 hit.
SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMsTIGR00409. proS_fam_II. 1 hit.
PROSITEPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameF0PQK2_BACT0
AccessionPrimary (citable) accession number: F0PQK2
Entry history
Integrated into UniProtKB/TrEMBL: May 3, 2011
Last sequence update: May 3, 2011
Last modified: May 1, 2013
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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