Histidyl-tRNA synthetase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P60906 (SYH_ECOLI)

Last modified June 16, 2009. Version 61. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Histidyl-tRNA synthetase
    EC=6.1.1.21
Alternative name(s):
    Histidine--tRNA ligase
      Short name=HisRS

Gene names

Name:	hisS
Ordered Locus Names:	b2514, JW2498

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	424 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-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). HAMAP MF_00127
Subunit structure	Homodimer. HAMAP MF_00127
Subcellular location	Cytoplasm. HAMAP MF_00127
Sequence similarities	Belongs to the class-II 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	histidyl-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 histidine-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

Removed HAMAP MF_00127

Chain

2 – 424

423

Histidyl-tRNA synthetase HAMAP MF_00127

PRO_0000136161

Secondary structure

424

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P60906-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: EBBA69DE488CB00D
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FASTA

424

47,029

        10         20         30         40         50         60 
MAKNIQAIRG MNDYLPGETA IWQRIEGTLK NVLGSYGYSE IRLPIVEQTP LFKRAIGEVT 

        70         80         90        100        110        120 
DVVEKEMYTF EDRNGDSLTL RPEGTAGCVR AGIEHGLLYN QEQRLWYIGP MFRHERPQKG 

       130        140        150        160        170        180 
RYRQFHQLGC EVFGLQGPDI DAELIMLTAR WWRALGISEH VTLELNSIGS LEARANYRDA 

       190        200        210        220        230        240 
LVAFLEQHKE KLDEDCKRRM YTNPLRVLDS KNPEVQALLN DAPALGDYLD EESREHFAGL 

       250        260        270        280        290        300 
CKLLESAGIA YTVNQRLVRG LDYYNRTVFE WVTNSLGSQG TVCAGGRYDG LVEQLGGRAT 

       310        320        330        340        350        360 
PAVGFAMGLE RLVLLVQAVN PEFKADPVVD IYLVASGADT QSAAMALAER LRDELPGVKL 

       370        380        390        400        410        420 
MTNHGGGNFK KQFARADKWG ARVAVVLGES EVANGTAVVK DLRSGEQTAV AQDSVAAHLR 


TLLG

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of histidine-tRNA synthetase and characterization of hisS transcripts." Freedman R., Gibson B., Donovan D., Biemann K., Eisenbeis S.J., Parker J., Schimmel P. J. Biol. Chem. 260:10063-10068(1985) [PubMed: 2991272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"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.
[5]	"The nucleotide sequence of the promoter region of hisS, the structural gene for histidyl-tRNA synthetase." Eisenbeis S.J., Parker J. Gene 18:107-114(1982) [PubMed: 6290315] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[6]	"Crystal structure of histidyl-tRNA synthetase from Escherichia coli complexed with histidyl-adenylate." Arnez J.G., Harris D.C., Mitschler A., Rees B., Francklyn C.S., Moras D. EMBO J. 14:4143-4155(1995) [PubMed: 7556055] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[7]	"The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase." Arnez J.G., Augustine J.G., Moras D., Francklyn C.S. Proc. Natl. Acad. Sci. U.S.A. 94:7144-7149(1997) [PubMed: 9207058] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).

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Cross-references

Sequence databases

M11843 Genomic DNA. Translation: AAA03226.1.
U00096 Genomic DNA. Translation: AAC75567.1.
AP009048 Genomic DNA. Translation: BAA16401.1.

PIR

SYECH. A23890.

RefSeq

AP_003100.1.
NP_417009.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1HTT	X-ray	2.60	A/B/C/D	1-424	[»]
1KMM	X-ray	2.60	A/B/C/D	1-424	[»]
1KMN	X-ray	2.80	A/B/C/D	1-424	[»]
2EL9	X-ray	2.70	A/B/C/D	1-424	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P60906.

ECO2DBASE

F048.1. 6TH EDITION.

Genome annotation databases

GeneID

946989.

GenomeReviews

Gene locus JW2498 in contig AP009048_GR.
Gene locus b2514 in contig U00096_GR.

KEGG

ecj:JW2498.
eco:b2514.

Organism-specific databases

EchoBASE

EB0448.

EcoGene

EG10453. hisS.

CMR

Search...

Phylogenomic databases

HOGENOM

P60906.

OMA

P60906. VFEWVTT.

Enzyme and pathway databases

BioCyc

EcoCyc:HISS-MON.
MetaCyc:HISS-MON.

Family and domain databases

HAMAP

MF_00127.
[Tree]

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-reg.
IPR006195. aa-tRNA-synth_II_cons-reg.
IPR004154. Anticodon_bd.
IPR015807. His-tRNA-synth_IIa_sub.
IPR004516. His-tRNA_synth_IIA.
[Graphical view]

Gene3D

G3DSA:3.40.50.800. Anticodon_bd. 1 hit.

PANTHER

PTHR11476. His-tRNA_synth. 1 hit.

Pfam

PF03129. HGTP_anticodon. 1 hit.
PF00587. tRNA-synt_2b. 1 hit.
[Graphical view]

PIRSF

PIRSF001549. His-tRNA_synth. 1 hit.

TIGRFAMs

TIGR00442. hisS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00131. Adenosine monophosphate.

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Entry information

Entry name

SYH_ECOLI

Accession

Primary (citable) accession number: P60906
Secondary accession number(s): P04804

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 61 of the entry and version 2 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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