SYH_SALTY
ID SYH_SALTY Reviewed; 424 AA.
AC O52765;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 134.
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=STM2522;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF PRO-117; SER-167;
RP ASN-254 AND ALA-302.
RC STRAIN=LT2;
RX PubMed=9671554; DOI=10.1006/jmbi.1998.1902;
RA Francklyn C.S., Adams J., Augustine J.;
RT "Catalytic defects in mutants of class II histidyl-tRNA synthetase from
RT Salmonella typhimurium previously linked to decreased control of histidine
RT biosynthesis regulation.";
RL J. Mol. Biol. 280:847-858(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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.
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; AF047040; AAC03121.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21416.1; -; Genomic_DNA.
DR RefSeq; NP_461457.1; NC_003197.2.
DR RefSeq; WP_001107141.1; NC_003197.2.
DR AlphaFoldDB; O52765; -.
DR SMR; O52765; -.
DR STRING; 99287.STM2522; -.
DR PaxDb; O52765; -.
DR EnsemblBacteria; AAL21416; AAL21416; STM2522.
DR GeneID; 1254044; -.
DR KEGG; stm:STM2522; -.
DR PATRIC; fig|99287.12.peg.2659; -.
DR HOGENOM; CLU_025113_1_1_6; -.
DR OMA; CDFDFIG; -.
DR PhylomeDB; O52765; -.
DR BioCyc; SENT99287:STM2522-MON; -.
DR BRENDA; 6.1.1.21; 5542.
DR SABIO-RK; O52765; -.
DR Proteomes; UP000001014; 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 1: Evidence at protein level;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..424
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136245"
FT MUTAGEN 117
FT /note="P->Q,S: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:9671554"
FT MUTAGEN 167
FT /note="S->F: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:9671554"
FT MUTAGEN 254
FT /note="N->T: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:9671554"
FT MUTAGEN 302
FT /note="A->T: Decrease in activity. Defect in histidine
FT binding."
FT /evidence="ECO:0000269|PubMed:9671554"
FT CONFLICT 422
FT /note="L -> Y (in Ref. 1; AAC03121)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 424 AA; 46927 MW; FF16198F837598E8 CRC64;
MAKNIQAIRG MNDYLPGETA IWQRIEGTLK NVLGSYGYSE IRLPIVEQTP LFKRAIGEVT
DVVEKEMYTF EDRNGDSLTL RPEGTAGCVR AGIEHGLLYN QEQRLWYIGP MFRHERPQKG
RYRQFHQLGA EVFGLQGPDI DAELIMLTAR WWRALGIAEH VSLELNSIGS LEARANYRDA
LVAFLEQHQE TLDEDCKRRM YTNPLRVLDS KNPDVQALLN DAPALGDYLD DDSREHFAGL
CKLLDAAGIA YTVNQRLVRG LDYYNRTVFE WVTNSLGSQG TVCAGGRYDG LVEQLGGRAT
PAVGFAMGLE RLVLLVQAVN PEFIASPVVD IYLVAAGAQT QSAAMTLAER LRDEMPGVKL
MTNHGGGNFK KQFARADKWG ARIALVLGES EVADGTVVVK DLRSGEQTAV AQDSVAAHLR
TLLG
