Glutaminyl-tRNA synthetase - Escherichia coli (strain K12)

Names and origin

Protein names

Recommended name:
    Glutaminyl-tRNA synthetase
    EC=6.1.1.18
Alternative name(s):
    Glutamine--tRNA ligase
      Short name=GlnRS

Gene names

Name:	glnS
Ordered Locus Names:	b0680, JW0666

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	554 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + L-glutamine + tRNA(Gln) = AMP + diphosphate + L-glutaminyl-tRNA(Gln). HAMAP MF_00126
Subunit structure	Monomer. HAMAP MF_00126
Subcellular location	Cytoplasm. HAMAP MF_00126
Sequence similarities	Belongs to the class-I aminoacyl-tRNA synthetase family.

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Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Aminoacyl-tRNA synthetase Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	glutaminyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro glutamyl-tRNA aminoacylation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: HAMAP glutamine-tRNA ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

Removed Ref.7 Ref.8

Chain

2 – 554

553

Glutaminyl-tRNA synthetase HAMAP MF_00126

PRO_0000195833

Regions

Motif

34 – 44

11

"HIGH" region HAMAP MF_00126

Motif

268 – 272

5

"KMSKS" region HAMAP MF_00126

Sites

Binding site

271

1

ATP By similarity

Experimental info

Sequence conflict

549 – 554

6

WAKVGE → GRK Ref.2

Secondary structure

1

.

554

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P00962-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: E720164EF990F335
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FASTA

554

63,478

        10         20         30         40         50         60 
MSEAEARPTN FIRQIIDEDL ASGKHTTVHT RFPPEPNGYL HIGHAKSICL NFGIAQDYKG 

        70         80         90        100        110        120 
QCNLRFDDTN PVKEDIEYVE SIKNDVEWLG FHWSGNVRYS SDYFDQLHAY AIELINKGLA 

       130        140        150        160        170        180 
YVDELTPEQI REYRGTLTQP GKNSPYRDRS VEENLALFEK MRAGGFEEGK ACLRAKIDMA 

       190        200        210        220        230        240 
SPFIVMRDPV LYRIKFAEHH QTGNKWCIYP MYDFTHCISD ALEGITHSLC TLEFQDNRRL 

       250        260        270        280        290        300 
YDWVLDNITI PVHPRQYEFS RLNLEYTVMS KRKLNLLVTD KHVEGWDDPR MPTISGLRRR 

       310        320        330        340        350        360 
GYTAASIREF CKRIGVTKQD NTIEMASLES CIREDLNENA PRAMAVIDPV KLVIENYQGE 

       370        380        390        400        410        420 
GEMVTMPNHP NKPEMGSRQV PFSGEIWIDR ADFREEANKQ YKRLVLGKEV RLRNAYVIKA 

       430        440        450        460        470        480 
ERVEKDAEGN ITTIFCTYDA DTLSKDPADG RKVKGVIHWV SAAHALPVEI RLYDRLFSVP 

       490        500        510        520        530        540 
NPGAADDFLS VINPESLVIK QGFAEPSLKD AVAGKAFQFE REGYFCLDSR HSTAEKPVFN 

       550 
RTVGLRDTWA KVGE

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity." Uemura H., Conley J., Yamao F., Rogers J., Soell D.G. Protein Seq. Data Anal. 1:479-485(1988) [PubMed: 2464170] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Escherichia coli glutaminyl-tRNA synthetase. I. Isolation and DNA sequence of the glnS gene." Yamao F., Inokuchi H., Cheung A., Ozeki H., Soell D.G. J. Biol. Chem. 257:11639-11643(1982) [PubMed: 6288695] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes." Hoben P., Uemura H., Yamao F., Cheung A., Swanson R., Sumner-Smith M., Soell D. Fed. Proc. 43:2972-2976(1984) [PubMed: 6389180] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[7]	"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: 9298646] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-13. Strain: K12 / EMG2.
[8]	"Escherichia coli glutaminyl-tRNA synthetase. II. Characterization of the glnS gene product." Hoben P., Royal N., Cheung A., Yamao F., Biemann K., Soell D. J. Biol. Chem. 257:11644-11650(1982) [PubMed: 6749844] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-6, CHARACTERIZATION. Strain: K12.
[9]	"Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8-A resolution." Rould M.A., Perona J.J., Soell D., Steitz T.A. Science 246:1135-1142(1989) [PubMed: 2479982] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[10]	"Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase." Rould M.A., Perona J.J., Steitz T.A. Nature 352:213-218(1991) [PubMed: 1857417] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[11]	"How glutaminyl-tRNA synthetase selects glutamine." Rath V.L., Silvian L.F., Beijer B., Sproat B.S., Steitz T.A. Structure 6:439-449(1998) [PubMed: 9562563] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).
[12]	"Influence of transfer RNA tertiary structure on aminoacylation efficiency by glutaminyl and cysteinyl-tRNA synthetases." Sherlin L.D., Bullock T.L., Newberry K.J., Lipman R.S., Hou Y.M., Beijer B., Sproat B.S., Perona J.J. J. Mol. Biol. 299:431-446(2000) [PubMed: 10860750] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

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Cross-references

Sequence databases

V01575 Genomic DNA. Translation: CAA24894.1.
U00096 Genomic DNA. Translation: AAC73774.1.
AP009048 Genomic DNA. Translation: BAA35328.1.
M16470, M16368 Genomic DNA. Translation: AAA69006.1.

PIR

SYECQT. G64802.
I41235.

RefSeq

AP_001318.1.
NP_415206.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EUQ	X-ray	3.10	A	1-548	[»]
1EUY	X-ray	2.60	A	1-548	[»]
1EXD	X-ray	2.70	A	2-547	[»]
1GSG	X-ray	2.80	P	2-554	[»]
1GTR	X-ray	2.50	A	2-554	[»]
1GTS	X-ray	2.80	A	2-553	[»]
1NYL	X-ray	2.60	A	9-546	[»]
1O0B	X-ray	2.70	A	2-553	[»]
1O0C	X-ray	2.70	A	2-553	[»]
1QRS	X-ray	2.60	A	2-553	[»]
1QRT	X-ray	2.70	A	2-553	[»]
1QRU	X-ray	3.00	A	2-553	[»]
1QTQ	X-ray	2.25	A	2-554	[»]
1ZJW	X-ray	2.50	A	2-553	[»]
2RD2	X-ray	2.60	A	1-548	[»]
2RE8	X-ray	2.60	A	1-548	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:9787N.

2-D gel databases

SWISS-2DPAGE

P00962.

ECO2DBASE

G061.0. 6TH EDITION.

Genome annotation databases

GeneID

945310.

GenomeReviews

Gene locus JW0666 in contig AP009048_GR.
Gene locus b0680 in contig U00096_GR.

KEGG

ecj:JW0666.
eco:b0680.

Organism-specific databases

EchoBASE

EB0385.

EcoGene

EG10390. glnS.

CMR

Search...

Phylogenomic databases

HOGENOM

P00962.

OMA

P00962. RMPTIAG.

Enzyme and pathway databases

BioCyc

EcoCyc:GLNS-MON.
MetaCyc:GLNS-MON.

BRENDA

6.1.1.18. 246.

Family and domain databases

HAMAP

MF_00126.
[Tree]

InterPro

IPR001412. aa-tRNA-synth_I_CS.
IPR004514. Gln-tRNA-synth_Ic.
IPR000924. Glu/Gln-tRNA-synth_Ic.
[Graphical view]

PANTHER

PTHR10119:SF3. GlnS. 1 hit.
PTHR10119. Glu_tRNA-synt_1c. 1 hit.

TIGRFAMs

TIGR00440. glnS. 1 hit.

PROSITE

PS00178. AA_TRNA_LIGASE_I. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

BindingDB

P00962.

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Entry information

Entry name

SYQ_ECOLI

Accession

Primary (citable) accession number: P00962
Secondary accession number(s): Q59403

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 111 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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