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Protein

Proline--tRNA ligase

Gene

proS

Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

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.UniRule annotation

Catalytic activityi

ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro).UniRule annotation

GO - Molecular functioni

  1. aminoacyl-tRNA editing activity Source: InterPro
  2. ATP binding Source: UniProtKB-HAMAP
  3. proline-tRNA ligase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. prolyl-tRNA aminoacylation Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Proline--tRNA ligaseUniRule annotation (EC:6.1.1.15UniRule annotation)
Alternative name(s):
Prolyl-tRNA synthetaseUniRule annotation
Short name:
ProRSUniRule annotation
Gene namesi
Name:proSUniRule annotation
Ordered Locus Names:c0235
OrganismiEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic identifieri199310 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000001410 Componenti: Chromosome

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Proline--tRNA ligasePRO_0000248692Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi199310.c0235.

Structurei

3D structure databases

ProteinModelPortaliQ8FKZ4.
SMRiQ8FKZ4. Positions 1-567.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

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

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000076893.
KOiK01881.
OMAiIQPAELW.
OrthoDBiEOG6TTVMR.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPiMF_01569. Pro_tRNA_synth_type1.
InterProiIPR002314. 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]
PANTHERiPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
PIRSFiPIRSF001535. ProRS_1. 1 hit.
PRINTSiPR01046. TRNASYNTHPRO.
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55826. SSF55826. 1 hit.
TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8FKZ4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGVRVL
60 70 80 90 100
KKVENIVREE MNNAGAIEVL MPVVQPSELW QESGRWEQYG PELLRIADRG
110 120 130 140 150
DRPFVLGPTH EEVITDLIRN ELSSYKQLPL NFYQIQTKFR DEVRPRFGVM
160 170 180 190 200
RSREFLMKDA YSFHTSQESL QETYDAMYAA YSKIFSRMGL DFRAVQADTG
210 220 230 240 250
SIGGSASHEF QVLAQSGEDD VVFSDTSDYA ANIELAEAIA PKEPRAAATQ
260 270 280 290 300
EMTLVDTPNA KTIAELVEQF NLPIEKTVKT LLVKAVEGSS FPLVALLVRG
310 320 330 340 350
DHELNEVKAE KLPQVASPLT FATEEEIRAV VKAGPGSLGP VNMPIPVVID
360 370 380 390 400
RTVAAMSDFA AGANIDGKHY FGINWDRDVA TPEIADIRNV VAGDPSPDGQ
410 420 430 440 450
GTLLIKRGIE VGHIFQLGTK YSEALKASVQ GEDGRNQILT MGCYGIGVTR
460 470 480 490 500
VVAAAIEQNY DERGIVWPDA IAPFQVAILP MNMHKSFRVQ ELAEKLYSEL
510 520 530 540 550
RAQGIEVLLD DRKERPGVMF ADMELIGIPH TIVLGDRNLD NDDIEYKYRR
560 570
NGEKQLIKTG DIVDYLVKQI KG
Length:572
Mass (Da):63,603
Last modified:September 5, 2006 - v2
Checksum:i153B48CE90AD1149
GO

Sequence cautioni

The sequence AAN78727.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN78727.1. Different initiation.
RefSeqiNP_752183.2. NC_004431.1.

Genome annotation databases

EnsemblBacteriaiAAN78727; AAN78727; c0235.
GeneIDi1037637.
KEGGiecc:c0235.
PATRICi18278537. VBIEscCol75197_0223.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014075 Genomic DNA. Translation: AAN78727.1. Different initiation.
RefSeqiNP_752183.2. NC_004431.1.

3D structure databases

ProteinModelPortaliQ8FKZ4.
SMRiQ8FKZ4. Positions 1-567.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi199310.c0235.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN78727; AAN78727; c0235.
GeneIDi1037637.
KEGGiecc:c0235.
PATRICi18278537. VBIEscCol75197_0223.

Phylogenomic databases

HOGENOMiHOG000076893.
KOiK01881.
OMAiIQPAELW.
OrthoDBiEOG6TTVMR.

Family and domain databases

Gene3Di3.40.50.800. 1 hit.
3.90.960.10. 1 hit.
HAMAPiMF_01569. Pro_tRNA_synth_type1.
InterProiIPR002314. 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]
PANTHERiPTHR11451:SF3. PTHR11451:SF3. 1 hit.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
PIRSFiPIRSF001535. ProRS_1. 1 hit.
PRINTSiPR01046. TRNASYNTHPRO.
SUPFAMiSSF52954. SSF52954. 1 hit.
SSF55826. SSF55826. 1 hit.
TIGRFAMsiTIGR00409. proS_fam_II. 1 hit.
PROSITEiPS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CFT073 / ATCC 700928 / UPEC.

Entry informationi

Entry nameiSYP_ECOL6
AccessioniPrimary (citable) accession number: Q8FKZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: April 1, 2015
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.