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

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P60906 (SYH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 97. History...

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

Documents (4) |

Third-party data

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

Names and origin

Protein names

Recommended name:
Histidine--tRNA ligase
EC=6.1.1.21

Alternative name(s):
Histidyl-tRNA synthetase
Short name=HisRS

Gene names

Name:	hisS
Ordered Locus Names:	b2514, JW2498

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

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

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

General annotation (Comments)

Catalytic activity	ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). HAMAP-Rule MF_00127
Subunit structure	Homodimer.
Subcellular location	Cytoplasm HAMAP-Rule MF_00127.
Sequence similarities	Belongs to the class-II aminoacyl-tRNA synthetase family.

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 Reference proteome
Gene Ontology (GO)
Biological_process	histidyl-tRNA aminoacylation Inferred from direct assay PubMed 4591623. Source: EcoCyc
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 direct assay PubMed 4591623. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed HAMAP-Rule MF_00127

Chain

2 – 424

423

Histidine--tRNA ligase HAMAP-Rule MF_00127

PRO_0000136161

Secondary structure

424

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P60906 [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

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
[6]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[7]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
[8]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

SYECH. A23890.

RefSeq

NP_417009.1. NC_000913.2.
YP_490742.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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

ProteinModelPortal

P60906.

SMR

P60906. Positions 4-424.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35894N.

IntAct

P60906. 2 interactions.

MINT

MINT-1236095.

STRING

511145.b2514.

2D gel databases

SWISS-2DPAGE

P60906.

Proteomic databases

PaxDb

P60906.

PRIDE

P60906.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75567; AAC75567; b2514.
BAA16401; BAA16401; BAA16401.

GeneID

12931595.
946989.

KEGG

ecj:Y75_p2467.
eco:b2514.

PATRIC

32120421. VBIEscCol129921_2613.

Organism-specific databases

EchoBASE

EB0448.

EcoGene

EG10453. hisS.

Phylogenomic databases

eggNOG

COG0124.

HOGENOM

HOG000018072.

K01892.

OMA

CGGGNFK.

ProtClustDB

PRK00037.

Enzyme and pathway databases

BioCyc

EcoCyc:HISS-MONOMER.
ECOL316407:JW2498-MONOMER.
MetaCyc:HISS-MONOMER.

SABIO-RK

P60906.

Gene expression databases

Genevestigator

P60906.

Family and domain databases

Gene3D

3.40.50.800. 1 hit.

HAMAP

MF_00127. His_tRNA_synth.

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR015807. His-tRNA-ligase.
IPR004516. HisRS/HisZ.
[Graphical view]

PANTHER

PTHR11476. PTHR11476. 1 hit.

Pfam

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

PIRSF

PIRSF001549. His-tRNA_synth. 1 hit.

SUPFAM

SSF52954. Anticodon_bd. 1 hit.

TIGRFAMs

TIGR00442. hisS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00131. Adenosine monophosphate.

EvolutionaryTrace

P60906.

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:	May 1, 2013
This is version 97 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Secondary structure

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

Other

Entry information

Relevant documents