ID   SYH_STAAW               Reviewed;         420 AA.
AC   P60912; O32422;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Histidine--tRNA ligase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=MW1581;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95446.1; -; Genomic_DNA.
DR   RefSeq; WP_000590826.1; NC_003923.1.
DR   AlphaFoldDB; P60912; -.
DR   SMR; P60912; -.
DR   EnsemblBacteria; BAB95446; BAB95446; BAB95446.
DR   KEGG; sam:MW1581; -.
DR   HOGENOM; CLU_025113_1_1_9; -.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000000418; Chromosome.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Disulfide bond; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..420
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136254"
FT   DISULFID        191..194
FT                   /evidence="ECO:0000250"
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