ID   SYH_ECOLI               Reviewed;         424 AA.
AC   P60906; P04804;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   04-NOV-2026, entry version 173.
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=b2514, JW2498;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=2991272; DOI=10.1016/s0021-9258(17)39212-8;
RA   Freedman R., Gibson B., Donovan D., Biemann K., Eisenbeis S.J., Parker J.,
RA   Schimmel P.;
RT   "Primary structure of histidine-tRNA synthetase and characterization of
RT   hisS transcripts.";
RL   J. Biol. Chem. 260:10063-10068(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA   Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA   Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA   Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA   Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT   "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT   genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT   its sequence features.";
RL   DNA Res. 4:91-113(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX   PubMed=6290315; DOI=10.1016/0378-1119(82)90108-1;
RA   Eisenbeis S.J., Parker J.;
RT   "The nucleotide sequence of the promoter region of hisS, the structural
RT   gene for histidyl-tRNA synthetase.";
RL   Gene 18:107-114(1982).
RN   [6]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY.
RX   PubMed=7556055; DOI=10.1002/j.1460-2075.1995.tb00088.x;
RA   Arnez J.G., Harris D.C., Mitschler A., Rees B., Francklyn C.S., Moras D.;
RT   "Crystal structure of histidyl-tRNA synthetase from Escherichia coli
RT   complexed with histidyl-adenylate.";
RL   EMBO J. 14:4143-4155(1995).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY.
RX   PubMed=9207058; DOI=10.1073/pnas.94.14.7144;
RA   Arnez J.G., Augustine J.G., Moras D., Francklyn C.S.;
RT   "The first step of aminoacylation at the atomic level in histidyl-tRNA
RT   synthetase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:7144-7149(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=tRNA(His) + L-histidine + ATP = L-histidyl-tRNA(His) + AMP +
CC         diphosphate + H(+); 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.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; M11843; AAA03226.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC75567.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16401.1; -; Genomic_DNA.
DR   PIR; A23890; SYECH.
DR   RefSeq; NP_417009.1; NC_000913.3.
DR   RefSeq; WP_001107167.1; NZ_CP009789.1.
DR   PDB; 1HTT; X-ray; 2.60 A; A/B/C/D=2-424.
DR   PDB; 1KMM; X-ray; 2.60 A; A/B/C/D=1-424.
DR   PDB; 1KMN; X-ray; 2.80 A; A/B/C/D=1-424.
DR   PDB; 2EL9; X-ray; 2.70 A; A/B/C/D=1-424.
DR   AlphaFoldDB; P60906; -.
DR   SMR; P60906; -.
DR   BioGRID; 4260589; 69.
DR   DIP; DIP-35894N; -.
DR   FunCoup; P60906; 765.
DR   IntAct; P60906; 2.
DR   STRING; 511145.b2514; -.
DR   DrugBank; DB03811; Histidinol.
DR   DrugBank; DB04201; Histidyl-Adenosine Monophosphate.
DR   jPOST; P60906; -.
DR   PaxDb; 511145-b2514; -.
DR   EnsemblBacteria; AAC75567; AAC75567; b2514.
DR   GeneID; 75172622; -.
DR   GeneID; 75206207; -.
DR   GeneID; 946989; -.
DR   KEGG; ecj:JW2498; -.
DR   KEGG; eco:b2514; -.
DR   KEGG; ecoc:C3026_13940; -.
DR   PATRIC; fig|1411691.4.peg.4222; -.
DR   EchoBASE; EB0448; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_1_1_6; -.
DR   InParanoid; P60906; -.
DR   OMA; AACENHF; -.
DR   OrthoDB; 9800814at2; -.
DR   PhylomeDB; P60906; -.
DR   BioCyc; EcoCyc:HISS-MONOMER; -.
DR   BioCyc; MetaCyc:HISS-MONOMER; -.
DR   BRENDA; 6.1.1.21; 2026.
DR   SABIO-RK; P60906; -.
DR   EvolutionaryTrace; P60906; -.
DR   PRO; PR:P60906; -.
DR   Proteomes; UP000000625; Chromosome.
DR   AbasyAtlas; P60906; -.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IDA:EcoCyc.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IDA:EcoCyc.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   CDD; cd00859; HisRS_anticodon; 1.
DR   FunFam; 3.30.930.10:FF:000005; Histidine--tRNA ligase; 1.
DR   FunFam; 3.40.50.800:FF:000007; Histidine--tRNA ligase; 1.
DR   Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR   Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 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   NCBIfam; TIGR00442; hisS; 1.
DR   PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm;
KW   Direct protein sequencing; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..424
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136161"
FT   HELIX           16..34
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   TURN            35..37
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          45..48
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           49..56
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          58..60
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           62..66
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          68..71
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          77..80
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           85..95
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          103..112
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          123..134
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           138..155
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           158..160
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          162..167
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           171..176
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           179..183
FT                   /evidence="ECO:0007829|PDB:1KMN"
FT   HELIX           225..227
FT                   /evidence="ECO:0007829|PDB:1KMM"
FT   HELIX           231..245
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   TURN            246..248
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          251..253
FT                   /evidence="ECO:0007829|PDB:1KMM"
FT   STRAND          260..262
FT                   /evidence="ECO:0007829|PDB:1KMM"
FT   STRAND          266..272
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   TURN            277..279
FT                   /evidence="ECO:0007829|PDB:2EL9"
FT   STRAND          281..287
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           291..294
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          302..308
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           309..319
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:1KMN"
FT   HELIX           324..327
FT                   /evidence="ECO:0007829|PDB:1KMM"
FT   STRAND          330..335
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           340..354
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          360..362
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           369..379
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          382..387
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           389..394
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          396..401
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   TURN            402..404
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   STRAND          407..411
FT                   /evidence="ECO:0007829|PDB:1HTT"
FT   HELIX           412..423
FT                   /evidence="ECO:0007829|PDB:1HTT"
SQ   SEQUENCE   424 AA;  47029 MW;  EBBA69DE488CB00D CRC64;
     MAKNIQAIRG MNDYLPGETA IWQRIEGTLK NVLGSYGYSE IRLPIVEQTP LFKRAIGEVT
     DVVEKEMYTF EDRNGDSLTL RPEGTAGCVR AGIEHGLLYN QEQRLWYIGP MFRHERPQKG
     RYRQFHQLGC EVFGLQGPDI DAELIMLTAR WWRALGISEH VTLELNSIGS LEARANYRDA
     LVAFLEQHKE KLDEDCKRRM YTNPLRVLDS KNPEVQALLN DAPALGDYLD EESREHFAGL
     CKLLESAGIA YTVNQRLVRG LDYYNRTVFE WVTNSLGSQG TVCAGGRYDG LVEQLGGRAT
     PAVGFAMGLE RLVLLVQAVN PEFKADPVVD IYLVASGADT QSAAMALAER LRDELPGVKL
     MTNHGGGNFK KQFARADKWG ARVAVVLGES EVANGTAVVK DLRSGEQTAV AQDSVAAHLR
     TLLG
//