ID   SYH_TREPA               Reviewed;         442 AA.
AC   O83647;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   25-MAY-2022, entry version 126.
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=TP_0641;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000520; AAC65615.1; -; Genomic_DNA.
DR   PIR; H71298; H71298.
DR   RefSeq; WP_010882086.1; NC_021490.2.
DR   AlphaFoldDB; O83647; -.
DR   SMR; O83647; -.
DR   IntAct; O83647; 17.
DR   STRING; 243276.TPANIC_0641; -.
DR   EnsemblBacteria; AAC65615; AAC65615; TP_0641.
DR   GeneID; 57879166; -.
DR   KEGG; tpa:TP_0641; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_12; -.
DR   OMA; YQIQKVW; -.
DR   OrthoDB; 277998at2; -.
DR   Proteomes; UP000000811; 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   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; 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; Reference proteome.
FT   CHAIN           1..442
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136286"
SQ   SEQUENCE   442 AA;  50199 MW;  079E2F89784D632B CRC64;
     MRVGSAVSPK VLKGFRDLLP DEEIERALLV EKLTVALRQM GFVPIDTPAL EYTEVLLRKS
     EGDTEKQMFR FVDKGGRDVA LRFDLTVPLA RFVATHYARL YFPFKRYHFA KVWRGEKPQM
     GRYREFTQCD FDIVGSDSVC ADFEILKSIR HMLYMAGAEH IRIHVAHRGL FDRFLRALSL
     SDQAEHILRI IDKRAKMAPH VLTAQLESLC DPVRVQKIMT YVSAGEVDGV APSFEHTLSA
     IETLTGGVSE ESTRLRKIYE LLCAVNIQSS YVFDPSITRG FDYYTGMVCE TFLTQLPHIG
     SVCSGGRYDH LTALYMKDAV SGVGASIGLD RLYAAFQQLG MSREHVCFVQ ALIFCQDSAL
     MDVYQKLCSY FAVQVATEVF PDPRKLSQQY AFAEKKGIRW GIFVEQRNAV VEDCLLVLRD
     LSTRKDTRLP AHEVRRRMAA EG