SYH_STAAU
ID SYH_STAAU Reviewed; 420 AA.
AC P60911; O32422;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Histidine--tRNA ligase;
DE EC=6.1.1.21;
DE AltName: Full=Histidyl-tRNA synthetase;
DE Short=HisRS;
GN Name=hisS;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=SR17238;
RX PubMed=9335275; DOI=10.1128/jb.179.20.6294-6301.1997;
RA Fujimura T., Murakami K.;
RT "Increase of methicillin resistance in Staphylococcus aureus caused by
RT deletion of a gene whose product is homologous to lytic enzymes.";
RL J. Bacteriol. 179:6294-6301(1997).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RX PubMed=10493797; DOI=10.1021/bi990482v;
RA Qiu X., Janson C.A., Blackburn M.N., Chhohan I.K., Hibbs M.,
RA Abdel-Meguid S.S.;
RT "Cooperative structural dynamics and a novel fidelity mechanism in
RT histidyl-tRNA synthetases.";
RL Biochemistry 38:12296-12304(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-
CC histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665,
CC Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21;
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; D76414; BAA23141.1; -; Genomic_DNA.
DR RefSeq; WP_000590826.1; NZ_WYDB01000002.1.
DR PDB; 1QE0; X-ray; 2.70 A; A/B=1-420.
DR PDBsum; 1QE0; -.
DR AlphaFoldDB; P60911; -.
DR SMR; P60911; -.
DR OMA; CDFDFIG; -.
DR BRENDA; 6.1.1.21; 3352.
DR EvolutionaryTrace; P60911; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 1.
DR Gene3D; 3.30.930.10; -; 1.
DR Gene3D; 3.40.50.800; -; 1.
DR HAMAP; MF_00127; His_tRNA_synth; 1.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
DR PANTHER; PTHR43707; PTHR43707; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW Disulfide bond; Ligase; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..420
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136249"
FT DISULFID 191..194
FT HELIX 13..33
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 82..91
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 94..96
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 101..111
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 123..133
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 137..153
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 159..165
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 169..183
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 192..196
FT /evidence="ECO:0007829|PDB:1QE0"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 231..245
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 262..272
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 279..291
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 302..309
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 310..319
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 331..336
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 338..353
FT /evidence="ECO:0007829|PDB:1QE0"
FT TURN 354..356
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 368..377
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 381..386
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 396..400
FT /evidence="ECO:0007829|PDB:1QE0"
FT TURN 401..403
FT /evidence="ECO:0007829|PDB:1QE0"
FT STRAND 406..409
FT /evidence="ECO:0007829|PDB:1QE0"
FT HELIX 413..419
FT /evidence="ECO:0007829|PDB:1QE0"
SQ SEQUENCE 420 AA; 48283 MW; 3B79521695278CA4 CRC64;
MIKIPRGTQD ILPEDSKKWR YIENQLDELM TFYNYKEIRT PIFESTDLFA RGVGDSTDVV
QKEMYTFKDK GDRSITLRPE GTAAVVRSYI EHKMQGNPNQ PIKLYYNGPM FRYERKQKGR
YRQFNQFGVE AIGAENPSVD AEVLAMVMHI YQSFGLKHLK LVINSVGDMA SRKEYNEALV
KHFEPVIHEF CSDCQSRLHT NPMRILDCKV DRDKEAIKTA PRITDFLNEE SKAYYEQVKA
YLDDLGIPYI EDPNLVRGLD YYTHTAFELM MDNPNYDGAI TTLCGGGRYN GLLELLDGPS
ETGIGFALSI ERLLLALEEE GIELDIEENL DLFIVTMGDQ ADRYAVKLLN HLRHNGIKAD
KDYLQRKIKG QMKQADRLGA KFTIVIGDQE LENNKIDVKN MTTGESETIE LDALVEYFKK
