SYH_ECOLI
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 03-AUG-2022, entry version 156.
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; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC 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 (2.6 ANGSTROMS).
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 (2.6 ANGSTROMS).
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=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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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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_STEB01000011.1.
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 PDBsum; 1HTT; -.
DR PDBsum; 1KMM; -.
DR PDBsum; 1KMN; -.
DR PDBsum; 2EL9; -.
DR AlphaFoldDB; P60906; -.
DR SMR; P60906; -.
DR BioGRID; 4260589; 66.
DR DIP; DIP-35894N; -.
DR IntAct; P60906; 2.
DR STRING; 511145.b2514; -.
DR DrugBank; DB03811; Histidinol.
DR DrugBank; DB04201; Histidyl-Adenosine Monophosphate.
DR SWISS-2DPAGE; P60906; -.
DR jPOST; P60906; -.
DR PaxDb; P60906; -.
DR PRIDE; P60906; -.
DR EnsemblBacteria; AAC75567; AAC75567; b2514.
DR EnsemblBacteria; BAA16401; BAA16401; BAA16401.
DR GeneID; 66673598; -.
DR GeneID; 946989; -.
DR KEGG; ecj:JW2498; -.
DR KEGG; eco:b2514; -.
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; CDFDFIG; -.
DR PhylomeDB; P60906; -.
DR BioCyc; EcoCyc:HISS-MON; -.
DR BioCyc; MetaCyc:HISS-MON; -.
DR BRENDA; 6.1.1.21; 2026.
DR SABIO-RK; P60906; -.
DR EvolutionaryTrace; P60906; -.
DR PRO; PR:P60906; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0006427; P:histidyl-tRNA aminoacylation; IDA:EcoCyc.
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 PANTHER; PTHR43707; PTHR43707; 1.
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 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 61..65
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..154
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 178..182
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 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
