ID   SYH_BORGP               Reviewed;         456 AA.
AC   Q662M6;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 102.
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=BG0137;
OS   Borrelia garinii subsp. bavariensis (strain ATCC BAA-2496 / DSM 23469 /
OS   PBi) (Borrelia bavariensis).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=290434;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2496 / DSM 23469 / PBi;
RX   PubMed=15547252; DOI=10.1093/nar/gkh953;
RA   Gloeckner G., Lehmann R., Romualdi A., Pradella S., Schulte-Spechtel U.,
RA   Schilhabel M., Wilske B., Suehnel J., Platzer M.;
RT   "Comparative analysis of the Borrelia garinii genome.";
RL   Nucleic Acids Res. 32:6038-6046(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; CP000013; AAU06995.1; -; Genomic_DNA.
DR   RefSeq; WP_011193488.1; NC_006156.1.
DR   AlphaFoldDB; Q662M6; -.
DR   SMR; Q662M6; -.
DR   STRING; 290434.BG0137; -.
DR   EnsemblBacteria; AAU06995; AAU06995; BG0137.
DR   KEGG; bga:BG0137; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_12; -.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000002276; 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..456
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136121"
SQ   SEQUENCE   456 AA;  52671 MW;  E58B47B84CD7F147 CRC64;
     MDVKTLKGFK DYLPKDSLIR IHIVKQIFSV LNSYNFDLID TPVLEYSELL LKKSGDESEK
     QIYRFKDHGG RDVSMRFDLT IPFARFVATN ISDLKFPFRR SQFGKVFRGE NSQKGRYREF
     MQFDFDIVGE DGFRADAEIL SVVYYGLEEI FLNFIEGINK KFIIHYSHLG ILNSFFEKLG
     IKEESIFILR NIDKIDKIGI DKVKEALLLK IEKEAVDSIL SLVNLQGAFK DKIQALKSIL
     GDNESVKRVE DVYRHLSLLK IQDSFNLNLK ISGGLDYYTG IVFESEVFGS NMGSVCSGGR
     YDNLVSSYSS SIQKVSGVGG SFGVDRIKDI IDLEQFSYIK IFVTKARSKV LIVNLDSALQ
     NYYYELATRF RNHDYSKVKN ISCEVYFKNK NGKNIKEQIE YALNKEIRFL VFVGQEEYKE
     NKIKVRDLTK KEELLLSFEE VINVIKCNEK LLCTPF