Proline--tRNA ligase - Escherichia coli (strain K12)

Contribute

Send feedback

Read comments (?) or add your own

P16659 (SYP_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 133. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Proline--tRNA ligase
EC=6.1.1.15

Alternative name(s):
Global RNA synthesis factor
Prolyl-tRNA synthetase
Short name=ProRS

Gene names

Name:	proS
Synonyms:	drpA
Ordered Locus Names:	b0194, JW0190

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	572 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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). Misacylated Cys-tRNA(Pro) is not edited by ProRS, but instead may be edited in trans by YbaK. HAMAP-Rule MF_01569
Catalytic activity	ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-tRNA(Pro). HAMAP-Rule MF_01569
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_01569.
Domain	Consists of three domains: the N-terminal catalytic domain, the editing domain and the C-terminal anticodon-binding domain. Ref.13
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family. ProS type 1 subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=0.25 mM for proline Ref.9 Ref.10 Ref.12 K_M=140 mM for alanine K_M=0.17 mM for cysteine

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	prolyl-tRNA aminoacylation Inferred from mutant phenotype PubMed 6991867. Source: EcoCyc
Cellular_component	cytosol Inferred from direct assay PubMed 16858726. Source: UniProtKB
Molecular_function	ATP binding Inferred from electronic annotation. Source: HAMAP Ala-tRNA(Pro) hydrolase activity Inferred from direct assay Ref.13. Source: UniProtKB proline-tRNA ligase activity Inferred from direct assay PubMed 9062123. Source: EcoCyc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
groL	P0A6F5	1	EBI-549550,EBI-543750

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 572

572

Proline--tRNA ligase HAMAP-Rule MF_01569

PRO_0000139329

Experimental info

Mutagenesis

257

T → A: Reduces the posttransfer editing activity 5-fold, with little change in both the aminoacylation and the pretransfer editing activities. Ref.11

Mutagenesis

279

K → A: Severely affects the posttransfer editing activity, with little change in both the aminoacylation and the pretransfer editing activities. Ref.11

Mutagenesis

350

D → A: Abolishes the pretransfer editing activity and reduces the aminoacylation activity 20-fold and the posttransfer editing activity 5-fold. Ref.11

Mutagenesis

369

H → A: Reduces both the aminoacylation and the pretransfer editing activities 2.5-fold, and the posttransfer editing activity 5-fold. Loss of specificity in deacylation. Ref.11

Mutagenesis

378

D → A: Little change in both the aminoacylation and the editing activities. Ref.11

Mutagenesis

386

D → A: Reduces the posttransfer editing activity approximately 2-fold, with little change in both the aminoacylation and the pretransfer editing activities. Ref.11

Mutagenesis

394

D → A: Reduces the posttransfer editing activity approximately 2-fold, with little change in both the aminoacylation and the pretransfer editing activities. Ref.11

Mutagenesis

443

C → G: 150-fold decrease in posttransfer editing activity against alanine, without change neither in pretransfer editing nor in aminoacylation. Ref.9

Sequence conflict

26 – 27

ML → IV Ref.1

Sequence conflict

127 – 128

QL → HV in AAA23710. Ref.2

Sequence conflict

205 – 216

SASHE…VLAQS → RPLTNSRCWRR in AAA23710. Ref.2

Sequence conflict

205

S → Q Ref.1

Sequence conflict

516 – 517

PG → RA Ref.2

Sequence conflict

518 – 572

Missing Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P16659 [UniParc].

Last modified August 29, 2003. Version 4.
Checksum: 312D29390E91C486
Show »

FASTA

572

63,693

        10         20         30         40         50         60 
MRTSQYLLST LKETPADAEV ISHQLMLRAG MIRKLASGLY TWLPTGVRVL KKVENIVREE 

        70         80         90        100        110        120 
MNNAGAIEVS MPVVQPADLW QESGRWEQYG PELLRFVDRG ERPFVLGPTH EEVITDLIRN 

       130        140        150        160        170        180 
ELSSYKQLPL NFYQIQTKFR DEVRPRFGVM RSREFLMKDA YSFHTSQESL QETYDAMYAA 

       190        200        210        220        230        240 
YSKIFSRMGL DFRAVQADTG SIGGSASHEF QVLAQSGEDD VVFSDTSDYA ANIELAEAIA 

       250        260        270        280        290        300 
PKEPRAAATQ EMTLVDTPNA KTIAELVEQF NLPIEKTVKT LLVKAVEGSS FPQVALLVRG 

       310        320        330        340        350        360 
DHELNEVKAE KLPQVASPLT FATEEEIRAV VKAGPGSLGP VNMPIPVVID RTVAAMSDFA 

       370        380        390        400        410        420 
AGANIDGKHY FGINWDRDVA TPEVADIRNV VAGDPSPDGQ GRLLIKRGIE VGHIFQLGTK 

       430        440        450        460        470        480 
YSEALKASVQ GEDGRNQILT MGCYGIGVTR VVAAAIEQNY DERGIVWPDA IAPFQVAILP 

       490        500        510        520        530        540 
MNMHKSFRVQ ELAEKLYSEL RAQGIEVLLD DRKERPGVMF ADMELIGIPH TIVLGDRNLD 

       550        560        570 
NDDIEYKYRR NGEKQLIKTG DIVEYLVKQI KG

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs." Eriani G., Delarue M., Poch O., Gangloff J., Moras D. Nature 347:203-206(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-12.
[2]	"Identification and sequence of the drpA gene from Escherichia coli." Zhou Z., Syvanen M. J. Bacteriol. 172:281-286(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Sequence of minutes 4-25 of Escherichia coli." Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W. Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 26-27; 205 AND 568-572. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	Miyamoto K. Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-155. Strain: K12.
[8]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[9]	"Hydrolytic editing by a class II aminoacyl-tRNA synthetase." Beuning P.J., Musier-Forsyth K. Proc. Natl. Acad. Sci. U.S.A. 97:8916-8920(2000) [PubMed] [Europe PMC] [Abstract] Cited for: EDITING ACTIVITY, KINETIC PARAMETERS, MUTAGENESIS OF CYS-443.
[10]	"Species-specific differences in amino acid editing by class II prolyl-tRNA synthetase." Beuning P.J., Musier-Forsyth K. J. Biol. Chem. 276:30779-30785(2001) [PubMed] [Europe PMC] [Abstract] Cited for: EDITING ACTIVITY, KINETIC PARAMETERS.
[11]	"Functional role of the prokaryotic proline-tRNA synthetase insertion domain in amino acid editing." Wong F.-C., Beuning P.J., Nagan M., Shiba K., Musier-Forsyth K. Biochemistry 41:7108-7115(2002) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF THR-257; LYS-279; ASP-350; HIS-369; ASP-378; ASP-386 AND ASP-394.
[12]	"Cysteine activation is an inherent in vitro property of prolyl-tRNA synthetases." Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H., Hartsch T., Soell D. J. Biol. Chem. 277:34743-34748(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PROLINE AND CYSTEINE ACTIVATION, EDITING ACTIVITY, KINETIC PARAMETERS.
[13]	"An isolated class II aminoacyl-tRNA synthetase insertion domain is functional in amino acid editing." Wong F.-C., Beuning P.J., Silvers C., Musier-Forsyth K. J. Biol. Chem. 278:52857-52864(2003) [PubMed] [Europe PMC] [Abstract] Cited for: EDITING DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X55518 Genomic DNA. Translation: CAA39134.1. M97858 Genomic DNA. Translation: AAA24420.1. M32357 Genomic DNA. Translation: AAA23710.1. U70214 Genomic DNA. Translation: AAB08622.1. U00096 Genomic DNA. Translation: AAC73305.1. AP009048 Genomic DNA. Translation: BAA77870.2. D15061 Genomic DNA. Translation: BAA03654.1.
PIR	YPEC. B64744.
RefSeq	NP_414736.1. NC_000913.2. YP_488497.1. NC_007779.1.
3D structure databases
ProteinModelPortal	P16659.
SMR	P16659. Positions 1-553.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-10573N.
IntAct	P16659. 20 interactions.
MINT	MINT-1261583.
STRING	511145.b0194.
2D gel databases
SWISS-2DPAGE	P16659.
Proteomic databases
PaxDb	P16659.
PRIDE	P16659.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAC73305; AAC73305; b0194. BAA77870; BAA77870; BAA77870.
GeneID	12932635. 949116.
KEGG	ecj:Y75_p0191. eco:b0194.
PATRIC	32115501. VBIEscCol129921_0202.
Organism-specific databases
EchoBASE	EB0763.
EcoGene	EG10770. proS.
Phylogenomic databases
eggNOG	COG0442.
HOGENOM	HOG000076893.
KO	K01881.
OMA	IQPAELW.
ProtClustDB	PRK09194.
Enzyme and pathway databases
BioCyc	EcoCyc:PROS-MONOMER. ECOL316407:JW0190-MONOMER. MetaCyc:PROS-MONOMER.
SABIO-RK	P16659.
Gene expression databases
Genevestigator	P16659.
Family and domain databases
Gene3D	3.40.50.800. 1 hit. 3.90.960.10. 1 hit.
HAMAP	MF_01569. Pro_tRNA_synth_type1.
InterPro	IPR002314. 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]
PANTHER	PTHR11451:SF3. PTHR11451:SF3. 1 hit.
Pfam	PF03129. HGTP_anticodon. 1 hit. PF00587. tRNA-synt_2b. 1 hit. PF04073. YbaK. 1 hit. [Graphical view]
PRINTS	PR01046. TRNASYNTHPRO.
SUPFAM	SSF52954. Anticodon_bd. 1 hit. SSF55826. YbaK/aa-tRNA-synth-assoc-reg. 1 hit.
TIGRFAMs	TIGR00409. proS_fam_II. 1 hit.
PROSITE	PS50862. AA_TRNA_LIGASE_II. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SYP_ECOLI

Accession

Primary (citable) accession number: P16659
Secondary accession number(s): P78272, Q59430

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	August 29, 2003
Last modified:	May 1, 2013
This is version 133 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Aminoacyl-tRNA synthetases

List of aminoacyl-tRNA synthetase entries

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents