ID   SYH_TROW8               Reviewed;         426 AA.
AC   Q83H72;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Probable histidine--tRNA ligase;
DE            EC=6.1.1.21;
DE   AltName: Full=Histidyl-tRNA synthetase;
DE            Short=HisRS;
GN   Name=hisS; OrderedLocusNames=TW794;
OS   Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC   Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=218496;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW08/27;
RX   PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA   Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA   Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA   Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA   Relman D.A.;
RT   "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT   Tropheryma whipplei.";
RL   Lancet 361:637-644(2003).
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; BX251412; CAD67453.1; -; Genomic_DNA.
DR   RefSeq; WP_011096731.1; NC_004551.1.
DR   AlphaFoldDB; Q83H72; -.
DR   SMR; Q83H72; -.
DR   GeneID; 67388575; -.
DR   KEGG; tws:TW794; -.
DR   HOGENOM; CLU_025113_3_0_11; -.
DR   OMA; YQIQKVW; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR015807; His-tRNA-ligase.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
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; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..426
FT                   /note="Probable histidine--tRNA ligase"
FT                   /id="PRO_0000136287"
SQ   SEQUENCE   426 AA;  48039 MW;  399623321706F64B CRC64;
     MKIVPPRGMQ DFLPHEKEHR DRITEVIYKS YISHGFNPIE TPSLENIERL ACGVGQENEK
     LTYKIIRRGL TGAQTVQHPD ELIDLGLRFD LTIPLVRFWN TNRARLPKIF RSLQIGHVWR
     AEKPQKGRRR QFIQCDIDII GQPEILAEIE LLVATLSTLE QLGIRTPKLH INDRRILFSM
     LNNLGVPHSC HVYVSIVLDK LRKIGLDLVK QELCEFPALV AYLASSVNSN TGSTDLCFDV
     SSTKDITHIR RTIQSALPHG CKFDCEDLCR IIASVNEFTQ TGVFFDPLLV RGMGYYTGPI
     FEILHDDYSI AGGGRYDGLV ERLGGLPTPA CGFSIGFERV LGLIKESVSL DPKKMILLYD
     PKVDPNLVVS VKLEFISKGF IVRPELASRS RRNQIELAKR EGFGAFLYLD PLSPPDGLLA
     KVKPIL