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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 23-JAN-2007, entry version 38.
DE Histidyl-tRNA synthetase (EC 6.1.1.21) (Histidine--tRNA ligase)
DE (HisRS).
GN Name=hisS; OrderedLocusNames=b2514, JW2498;
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX MEDLINE=85261421; PubMed=2991272;
RA Freedman R., Gibson B., Donovan D., Biemann K., Eisenbeis S.J.,
RA Parker J., Schimmel P.;
RT "Primary structure of histidine-tRNA synthetase and characterization
RT of 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 MEDLINE=97349980; PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
RA Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
RA Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
RA Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
RA Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
RA Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-
RT K12 genome corresponding to 50.0-68.8 min on the linkage map and
RT analysis of 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 MEDLINE=97426617; 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.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1474(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
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16.
RX MEDLINE=83028525; 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
RT structural gene for histidyl-tRNA synthetase.";
RL Gene 18:107-114(1982).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX MEDLINE=96016186; PubMed=7556055;
RA Arnez J.G., Harris D.C., Mitschler A., Rees B., Francklyn C.S.,
RA 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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
RX MEDLINE=97352765; 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: ATP + L-histidine + tRNA(His) = AMP +
CC diphosphate + L-histidyl-tRNA(His).
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC family.
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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 PDB; 1HTT; X-ray; A/B/C/D=1-424.
DR PDB; 1KMM; X-ray; A/B/C/D=1-424.
DR PDB; 1KMN; X-ray; A/B/C/D=1-424.
DR IntAct; P60906; -.
DR SWISS-2DPAGE; P60906; COLI.
DR ECO2DBASE; F048.1; 6TH EDITION.
DR GenomeReviews; U00096_GR; b2514.
DR GenomeReviews; AP009048_GR; JW2498.
DR KEGG; ecj:JW2498; -.
DR KEGG; eco:b2514; -.
DR EchoBASE; EB0448; -.
DR EcoGene; EG10453; hisS.
DR LinkHub; P60906; -.
DR HAMAP; MF_00127; -; 1.
DR InterPro; IPR004154; Anticodon_bd.
DR InterPro; IPR004516; HisS.
DR InterPro; IPR002314; tRNA-synt_2b.
DR InterPro; IPR006195; tRNA_ligase_II.
DR Gene3D; G3DSA:3.40.50.800; Anticodon_bd; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR TIGRFAMs; TIGR00442; hisS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding;
KW Complete proteome; Direct protein sequencing; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 424 Histidyl-tRNA synthetase.
FT /FTId=PRO_0000136161.
FT TURN 9 10
FT HELIX 16 34
FT TURN 35 37
FT STRAND 45 48
FT HELIX 49 56
FT STRAND 58 60
FT HELIX 61 65
FT TURN 66 66
FT STRAND 68 71
FT TURN 73 74
FT STRAND 77 80
FT HELIX 85 95
FT TURN 96 96
FT TURN 99 100
FT STRAND 103 112
FT STRAND 123 134
FT HELIX 138 154
FT TURN 155 156
FT HELIX 158 160
FT STRAND 162 167
FT HELIX 171 176
FT HELIX 231 245
FT TURN 246 248
FT TURN 255 256
FT TURN 262 263
FT STRAND 266 272
FT STRAND 281 287
FT TURN 289 290
FT HELIX 291 294
FT TURN 295 296
FT STRAND 302 308
FT HELIX 309 319
FT TURN 321 322
FT STRAND 330 335
FT TURN 338 339
FT HELIX 340 354
FT TURN 356 357
FT STRAND 360 362
FT HELIX 369 379
FT TURN 380 380
FT STRAND 382 387
FT HELIX 389 394
FT TURN 395 395
FT STRAND 396 401
FT TURN 402 404
FT STRAND 407 411
FT HELIX 412 423
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
//