SYH_YERPE
ID SYH_YERPE Reviewed; 424 AA.
AC Q8ZCT6; Q0WD25; Q8D0Z2;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 134.
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};
GN OrderedLocusNames=YPO2878, y1354, YP_2744;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(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; AL590842; CAL21489.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84927.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS62932.1; -; Genomic_DNA.
DR PIR; AF0350; AF0350.
DR RefSeq; WP_002209816.1; NZ_WHLN01000027.1.
DR RefSeq; YP_002347813.1; NC_003143.1.
DR AlphaFoldDB; Q8ZCT6; -.
DR SMR; Q8ZCT6; -.
DR IntAct; Q8ZCT6; 1.
DR STRING; 214092.YPO2878; -.
DR PaxDb; Q8ZCT6; -.
DR DNASU; 1146301; -.
DR EnsemblBacteria; AAM84927; AAM84927; y1354.
DR EnsemblBacteria; AAS62932; AAS62932; YP_2744.
DR GeneID; 66844737; -.
DR KEGG; ype:YPO2878; -.
DR KEGG; ypk:y1354; -.
DR KEGG; ypm:YP_2744; -.
DR PATRIC; fig|214092.21.peg.3324; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_1_1_6; -.
DR OMA; CDFDFIG; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; 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; IBA:GO_Central.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..424
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136305"
FT CONFLICT 89
FT /note="V -> A (in Ref. 2; AAM84927)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 47262 MW; B6DAD3B591E6703D CRC64;
MAKNIQAIRG MNDYLPADTA IWQRIESILK QVLSGYGYSE IRMPIVEQTP LFKRAIGEVT
DVVEKEMYTF DDRNGESLTL RPEGTAGCVR AGIEHGLLYN QEQRLWYIGP MFRYERPQKG
RYRQFHQLGA EVFGLPGPDI DAELILLTAR WWRALGIFEH VKLELNSIGS LAARADYREA
LVAFLEQHVE VLDEDCKRRM YSNPLRVLDS KNPDVQQLLD DAPKLSDYLD EESKQHFAGL
CELLDKASIP YTVNERLVRG LDYYNRTVFE WVTHSLGAQG TVCAGGRYDG LVEQLGGRAT
PAVGFAMGLE RLVLLVQAVN ADFQVPATVD AYVISSGEGA QSAAMLLAES LRDALPTLKI
MTNYGGGNVK KQFTRADKWG ARVALMLGES EVAAQQVVVK DLRNGEQETL AQADVAARLA
LMLG
