ID   SYH_BARHE               Reviewed;         495 AA.
AC   Q6G289;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=BH13610;
OS   Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS   (Rochalimaea henselae).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bartonellaceae; Bartonella.
OX   NCBI_TaxID=283166;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
RX   PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA   Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA   Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA   La Scola B., Holmberg M., Andersson S.G.E.;
RT   "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT   of the zoonotic agent Bartonella henselae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897699; CAF28134.1; -; Genomic_DNA.
DR   RefSeq; WP_011181157.1; NZ_LRIJ02000001.1.
DR   AlphaFoldDB; Q6G289; -.
DR   SMR; Q6G289; -.
DR   STRING; 283166.BH13610; -.
DR   PaxDb; Q6G289; -.
DR   PRIDE; Q6G289; -.
DR   EnsemblBacteria; CAF28134; CAF28134; BH13610.
DR   GeneID; 64157529; -.
DR   KEGG; bhe:BH13610; -.
DR   eggNOG; COG0124; Bacteria.
DR   OMA; CDFDFIG; -.
DR   Proteomes; UP000000421; 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..495
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136111"
SQ   SEQUENCE   495 AA;  55479 MW;  A7013E8E55F1CB2F CRC64;
     MSSKQEKTKA RLPRGFVDRT SAQLYAIEVM IAQIRQVYEL YGFEALETPI FEYTDVLGKF
     LPDEDRPNAG VFSLQDDDEQ WMSLRYDLTA PLARYFSENF ETLPKPYRSY RLGFVFRNEK
     PGPGRFRQFM QFDADIVGTP TVAADAEICM MAADSLQKLG FQHHDYVIRL NNRKILDAVL
     EKVGLAGSEQ AQRRLTVLRA IDKLDKFGLE GVRLLLGKGR LDESGDFTKG AELKDKEIDG
     ILSLLTIEVG TAEETFDALR KIVDQSEEGL EGVRELEEMQ AIFAENDTQN RIKIDPSVVR
     GLEYYTGPVF EAALLFDVLN DDGQKVVFGS VGGGGRYDGL VARFRGENIP ATGFSIGVSR
     LIAALQNLGK LPVKEKTGPV VVLMMDKEPE IVARYQKMVM QLRSAGIPAE LYLGASGMKA
     QMKYADRRQA PCVVIQGSQE RESGTIQIKD LVEGARLSHE IKDNQTWRES RPAQVTVDEE
     QLVKTVQDIL AAQKR