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Reviewed, UniProtKB/Swiss-Prot B7GWV6 (SYP_ACIB3)

Last modified July 28, 2009. Version 7. 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: ABBFA_000643
OrganismAcinetobacter baumannii (strain AB307-0294) [Complete proteome] [HAMAP]
Taxonomic identifier557600 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length571 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Catalytic activity

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

Subunit structure

Homodimer By similarity.

Subcellular location

Cytoplasm By similarity.

Domain

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

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 – 571571Prolyl-tRNA synthetase HAMAP MF_01569
PRO_1000199341

Sequences

Sequence LengthMass (Da)Tools
B7GWV6-1 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: F157F4BEB475EA85

FASTA57163,275
        10         20         30         40         50         60 
MRASRFLFAT LRETPNDAEV ISHQLMLRAG MIRKLASGLY TWLPMGTRVL KKVDAIVREE 

        70         80         90        100        110        120 
MNRSGAMEVF MPVTQPASLW EESGRYEQYG PELLRFKDRH DNPFVLGPTH EEVITDLARN 

       130        140        150        160        170        180 
ELKSYKQLPV NFYQIQTKFR DEIRPRFGVM RSREFIMKDA YSFHATQESL QETYDVMYDT 

       190        200        210        220        230        240 
YSRIFTRLGL DFRPVQADTG SIGGSASHEF HVLAASGEDD IAFSTESDYA ANVEMAEAVL 

       250        260        270        280        290        300 
VGERAAPTQE FKLVETPNQK TIADVCQFLN ADPKQSVKAL LVQGVADEKG NVPVVALFLR 

       310        320        330        340        350        360 
GDHELNEIKA EKHPLVAAPL AFATEEQLQA FGLTAGFTGP QGLVEKGITV IVDRAASVLS 

       370        380        390        400        410        420 
DFVAGANEAD KHAIGVNWER DAQITEVFDL RNVVEGDPSP DGKGTLQIKR GIEVGHIFQL 

       430        440        450        460        470        480 
GTKYSEALGC KVLGEDGKPF TVTMGCYGIG VTRVVAAAIE QNYDDKGIIW PQAIAPFEIA 

       490        500        510        520        530        540 
IVPMNAHKSP RTLEAAEALY AELQAQGFDV LLDDRNERPG VKFSDLELMG IPHRIVIGEK 

       550        560        570 
GLDAGTFEYK GRRDAEASNL TKEELLAKLA R 

« Hide

References

[1]"Comparative genome sequence analysis of multidrug-resistant Acinetobacter baumannii."
Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J., MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M., Bonomo R.A., Gill S.R.
J. Bacteriol. 190:8053-8064(2008) [PubMed: 18931120] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP001172 Genomic DNA. Translation: ACJ56792.1.
RefSeqYP_002324567.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID7057551.
GenomeReviewsGene locus ABBFA_000643 in contig CP001172_GR.
KEGGabb:ABBFA_000643.

Organism-specific databases

CMRSearch...

Family and domain databases

HAMAPMF_01569.
[Tree]
InterProIPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR004500. Pro-tRNA-synth_IIa_bac.
IPR002316. Pro-tRNA-synth_IIa_cons-reg.
IPR007214. YbaK/aa-tRNA-synth-assoc-reg.
[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_ACIB3
AccessionPrimary (citable) accession number: B7GWV6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: July 28, 2009
This is version 7 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