ID   SYH_HELP2               Reviewed;         442 AA.
AC   B6JN30;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=Histidine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00127};
DE            EC=6.1.1.21 {ECO:0000255|HAMAP-Rule:MF_00127};
DE   AltName: Full=Histidyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00127};
DE            Short=HisRS {ECO:0000255|HAMAP-Rule:MF_00127};
GN   Name=hisS {ECO:0000255|HAMAP-Rule:MF_00127}; OrderedLocusNames=HPP12_1156;
OS   Helicobacter pylori (strain P12).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=570508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P12;
RA   Fischer W., Windhager L., Karnholz A., Zeiller M., Zimmer R., Haas R.;
RT   "The complete genome sequence of Helicobacter pylori strain P12.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000255|HAMAP-Rule:MF_00127};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00127}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00127}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00127}.
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DR   EMBL; CP001217; ACJ08308.1; -; Genomic_DNA.
DR   RefSeq; WP_000632521.1; NC_011498.1.
DR   AlphaFoldDB; B6JN30; -.
DR   SMR; B6JN30; -.
DR   EnsemblBacteria; ACJ08308; ACJ08308; HPP12_1156.
DR   KEGG; hpp:HPP12_1156; -.
DR   HOGENOM; CLU_025113_3_0_7; -.
DR   OMA; CDFDFIG; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000008198; 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   CDD; cd00859; HisRS_anticodon; 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   InterPro; IPR033656; HisRS_anticodon.
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; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..442
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_1000095560"
SQ   SEQUENCE   442 AA;  50419 MW;  1D61D34A91890289 CRC64;
     MITPKVLSGF KDRLPKDAIQ KAQLLAKVSV VFQSFGFVPI ETPHLEYAQT LLPDTSSDIQ
     KEIYRFKDHG DRDVALRFDL TVPLARFVSL HHQILGMPFK RYAIGNVFRG ERAQKGRYRE
     FTQCDFDFIG SESLVCDAEI IQVIIASLKA LDLEDFCVSI NHRKILNGIC EYFRISQVNE
     ALRIVDKLEK IGLDGVEEEL KKECDLNSNT IKELLEMVQI KQNDLSHAEF FEKIAYLKDY
     NENLKKGIQD LERLYQLLGD LQISQNLYKI DFSIARGLGY YTGIVYETTL NEMKSLGSVC
     SGGRYDHLTK NFSKENLQGV GASIGIDRLI VALSEMQLLD ERSTQAKVLI ACMHEEYFSY
     ANRLAESLRQ SGIFSEVYPE AQKIKKPFSY ANHRGHEFVA VIGEEEFKSE TLSLKNMHSG
     MQLNCLSFLK ALEIIGENDE DL