P60911 (SYH_STAAU) Reviewed, UniProtKB/Swiss-Prot

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

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	420 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). HAMAP MF_00127
Subunit structure	Homodimer By similarity. HAMAP MF_00127
Subcellular location	Cytoplasm HAMAP 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
PTM	Disulfide bond
Technical term	3D-structure
Gene Ontology (GO)
Biological process	histidyl-tRNA aminoacylation Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW histidine-tRNA ligase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 420

420

Histidine--tRNA ligase HAMAP MF_00127

PRO_0000136249

Amino acid modifications

Disulfide bond

191 ↔ 194

HAMAP MF_00127

Secondary structure

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420

Helix Strand Turn

Details...

Helix

13 – 33

21

Beta strand

42 – 45

4

Helix

46 – 49

4

Beta strand

65 – 67

3

Helix

69 – 72

4

Beta strand

75 – 77

3

Helix

82 – 91

10

Helix

94 – 96

3

Beta strand

101 – 111

11

Beta strand

123 – 133

11

Helix

137 – 153

17

Beta strand

159 – 165

7

Helix

169 – 183

15

Helix

184 – 189

6

Helix

192 – 196

5

Turn

197 – 200

4

Helix

202 – 205

4

Helix

223 – 225

3

Helix

231 – 245

15

Beta strand

262 – 272

11

Beta strand

279 – 291

13

Helix

292 – 295

4

Beta strand

302 – 309

8

Helix

310 – 319

10

Beta strand

331 – 336

6

Helix

338 – 353

16

Turn

354 – 356

3

Beta strand

359 – 361

3

Helix

368 – 377

10

Beta strand

381 – 386

6

Helix

388 – 393

6

Beta strand

396 – 400

5

Turn

401 – 403

3

Beta strand

406 – 409

4

Helix

413 – 419

7

Sequences

	Sequence		Length	Mass (Da)
	P60911 [UniParc]. Last modified April 13, 2004. Version 1. Checksum: 3B79521695278CA4	FASTA	420	48,283
	10 20 30 40 50 60 MIKIPRGTQD ILPEDSKKWR YIENQLDELM TFYNYKEIRT PIFESTDLFA RGVGDSTDVV 70 80 90 100 110 120 QKEMYTFKDK GDRSITLRPE GTAAVVRSYI EHKMQGNPNQ PIKLYYNGPM FRYERKQKGR 130 140 150 160 170 180 YRQFNQFGVE AIGAENPSVD AEVLAMVMHI YQSFGLKHLK LVINSVGDMA SRKEYNEALV 190 200 210 220 230 240 KHFEPVIHEF CSDCQSRLHT NPMRILDCKV DRDKEAIKTA PRITDFLNEE SKAYYEQVKA 250 260 270 280 290 300 YLDDLGIPYI EDPNLVRGLD YYTHTAFELM MDNPNYDGAI TTLCGGGRYN GLLELLDGPS 310 320 330 340 350 360 ETGIGFALSI ERLLLALEEE GIELDIEENL DLFIVTMGDQ ADRYAVKLLN HLRHNGIKAD 370 380 390 400 410 420 KDYLQRKIKG QMKQADRLGA KFTIVIGDQE LENNKIDVKN MTTGESETIE LDALVEYFKK

References

[1]	"Increase of methicillin resistance in Staphylococcus aureus caused by deletion of a gene whose product is homologous to lytic enzymes." Fujimura T., Murakami K. J. Bacteriol. 179:6294-6301(1997) [PubMed: 9335275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: SR17238.
[2]	"Cooperative structural dynamics and a novel fidelity mechanism in histidyl-tRNA synthetases." Qiu X., Janson C.A., Blackburn M.N., Chhohan I.K., Hibbs M., Abdel-Meguid S.S. Biochemistry 38:12296-12304(1999) [PubMed: 10493797] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

D76414 Genomic DNA. Translation: BAA23141.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QE0	X-ray	2.70	A/B	1-420	[»]

ProteinModelPortal

P60911.

SMR

P60911. Positions 1-420.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

6.1.1.21. 5870.

Family and domain databases

HAMAP

MF_00127. His_tRNA_synth.
[Tree]

InterPro

IPR002314. aa-tRNA-synt_IIb_cons-dom.
IPR006195. aa-tRNA-synth_II.
IPR004154. Anticodon-bd.
IPR015807. His-tRNA-synth_IIa_subgr.
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.

SUPFAM

SSF52954. Anticodon_bd. 1 hit.

TIGRFAMs

TIGR00442. HisS. 1 hit.

PROSITE

PS50862. AA_TRNA_LIGASE_II. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SYH_STAAU

Accession

Primary (citable) accession number: P60911
Secondary accession number(s): O32422

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 13, 2004
Last sequence update:	April 13, 2004
Last modified:	January 25, 2012
This is version 49 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program