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Protein

Proline--tRNA ligase

Gene

proS

Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminoacyl-tRNA synthetase, Ligase

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-2331-MONOMER.
BRENDAi6.1.1.15. 2095.

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:EF_2379
OrganismiEnterococcus faecalis (strain ATCC 700802 / V583)
Taxonomic identifieri226185 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus
Proteomesi
  • UP000001415 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 572572Proline--tRNA ligasePRO_0000248688Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

DIPiDIP-29057N.
STRINGi226185.EF2379.

Structurei

Secondary structure

1
572
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53Combined sources
Helixi21 – 288Combined sources
Beta strandi31 – 366Combined sources
Beta strandi39 – 424Combined sources
Helixi44 – 6219Combined sources
Turni63 – 653Combined sources
Beta strandi73 – 764Combined sources
Helixi78 – 836Combined sources
Helixi85 – 884Combined sources
Beta strandi95 – 973Combined sources
Beta strandi103 – 1064Combined sources
Helixi111 – 12111Combined sources
Helixi125 – 1273Combined sources
Beta strandi130 – 13910Combined sources
Helixi148 – 1503Combined sources
Beta strandi153 – 16614Combined sources
Helixi167 – 18721Combined sources
Beta strandi192 – 1965Combined sources
Helixi199 – 2024Combined sources
Beta strandi205 – 2139Combined sources
Beta strandi218 – 22811Combined sources
Beta strandi230 – 2323Combined sources
Turni233 – 2353Combined sources
Beta strandi253 – 2564Combined sources
Helixi263 – 2708Combined sources
Helixi274 – 2763Combined sources
Beta strandi277 – 2859Combined sources
Beta strandi288 – 2958Combined sources
Helixi302 – 3098Combined sources
Beta strandi314 – 3163Combined sources
Helixi319 – 3268Combined sources
Helixi330 – 3323Combined sources
Beta strandi335 – 3373Combined sources
Beta strandi343 – 3475Combined sources
Turni348 – 3525Combined sources
Beta strandi355 – 3595Combined sources
Beta strandi365 – 3706Combined sources
Turni372 – 3743Combined sources
Beta strandi379 – 3824Combined sources
Beta strandi396 – 41520Combined sources
Helixi417 – 4226Combined sources
Beta strandi425 – 4273Combined sources
Beta strandi433 – 4353Combined sources
Beta strandi437 – 4448Combined sources
Helixi445 – 45612Combined sources
Turni466 – 4683Combined sources
Beta strandi472 – 4787Combined sources
Helixi483 – 49816Combined sources
Beta strandi503 – 5064Combined sources
Helixi512 – 52211Combined sources
Beta strandi525 – 5306Combined sources
Helixi532 – 5365Combined sources
Beta strandi538 – 5436Combined sources
Turni544 – 5463Combined sources
Beta strandi549 – 5535Combined sources
Helixi554 – 56411Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J3LX-ray2.30A/B1-572[»]
2J3MX-ray2.30A/B1-572[»]
ProteinModelPortaliQ831W7.
SMRiQ831W7. Positions 1-570.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ831W7.

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

eggNOGiENOG4105C90. Bacteria.
COG0442. LUCA.
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.
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. 2 hits.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
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.

Q831W7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQSKMLIPT LREVPNDAEV LSHQILLRAG YIRQVAAGIY SYLPLANRVL
60 70 80 90 100
EKLKTIMREE FEKIDAVEML MPALLPAELW KESGRYETYG PNLYRLKDRN
110 120 130 140 150
DRDYILGPTH EETFTELIRD EINSYKRLPL NLYQIQTKYR DEKRSRSGLL
160 170 180 190 200
RGREFIMKDG YSFHADEASL DQSYRDYEKA YSRIFERCGL EFRAIIGDGG
210 220 230 240 250
AMGGKDSKEF MAISEIGEDT ICYSTESDYA ANLEMATSLY TPKKSHETQL
260 270 280 290 300
DLEKIATPEV GTIAEVANFF EVEPQRIIKS VLFIADEEPV MVLVRGDHDV
310 320 330 340 350
NDVKLKNFLG ADFLDEATEE DARRVLGAGF GSIGPVNVSE DVKIYADLAV
360 370 380 390 400
QDLANAIVGA NEDGYHLTNV NPDRDFQPIS YEDLRFVQEG DPSPDGNGVL
410 420 430 440 450
AFTKGIEIGH IFKLGTRYSD AMGATVLDEN GREKSVIMGC YGIGVSRLLS
460 470 480 490 500
AIVEQNADER GINWPTGIAP FDLHVVQMNV KDEYQTKLSQ EVEAMMTEAG
510 520 530 540 550
YEVLVDDRNE RAGVKFADAD LIGCPIRITV GKKAVDGVVE VKIKRTGEML
560 570
EVRKEELEST LSILMNTTSE VE
Length:572
Mass (Da):64,267
Last modified:June 1, 2003 - v1
Checksum:iD2267BE6E4A85998
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO82100.1.
RefSeqiNP_816030.1. NC_004668.1.
WP_002382780.1. NZ_KE136528.1.

Genome annotation databases

EnsemblBacteriaiAAO82100; AAO82100; EF_2379.
GeneIDi1201247.
KEGGiefa:EF2379.
PATRICi21855011. VBIEntFae7065_2226.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016830 Genomic DNA. Translation: AAO82100.1.
RefSeqiNP_816030.1. NC_004668.1.
WP_002382780.1. NZ_KE136528.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J3LX-ray2.30A/B1-572[»]
2J3MX-ray2.30A/B1-572[»]
ProteinModelPortaliQ831W7.
SMRiQ831W7. Positions 1-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29057N.
STRINGi226185.EF2379.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAO82100; AAO82100; EF_2379.
GeneIDi1201247.
KEGGiefa:EF2379.
PATRICi21855011. VBIEntFae7065_2226.

Phylogenomic databases

eggNOGiENOG4105C90. Bacteria.
COG0442. LUCA.
KOiK01881.
OMAiIQPAELW.
OrthoDBiEOG6TTVMR.

Enzyme and pathway databases

BioCyciEFAE226185:GHI1-2331-MONOMER.
BRENDAi6.1.1.15. 2095.

Miscellaneous databases

EvolutionaryTraceiQ831W7.

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.
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. 2 hits.
PfamiPF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
PF04073. tRNA_edit. 1 hit.
[Graphical view]
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: ATCC 700802 / V583.

Entry informationi

Entry nameiSYP_ENTFA
AccessioniPrimary (citable) accession number: Q831W7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: June 1, 2003
Last modified: November 11, 2015
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Aminoacyl-tRNA synthetases
    List of aminoacyl-tRNA synthetase entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.