SYH_BORBU
ID SYH_BORBU Reviewed; 456 AA.
AC O51160;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 25-MAY-2022, entry version 127.
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=BB_0135;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; AE000783; AAC66531.2; -; Genomic_DNA.
DR PIR; G70116; G70116.
DR RefSeq; NP_212269.2; NC_001318.1.
DR RefSeq; WP_002656264.1; NC_001318.1.
DR AlphaFoldDB; O51160; -.
DR SMR; O51160; -.
DR STRING; 224326.BB_0135; -.
DR PRIDE; O51160; -.
DR EnsemblBacteria; AAC66531; AAC66531; BB_0135.
DR GeneID; 56568083; -.
DR KEGG; bbu:BB_0135; -.
DR PATRIC; fig|224326.49.peg.533; -.
DR HOGENOM; CLU_025113_3_0_12; -.
DR OMA; YQIQKVW; -.
DR Proteomes; UP000001807; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
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 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..456
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136120"
SQ SEQUENCE 456 AA; 52718 MW; 16FF8083798BF319 CRC64;
MDIKTLKGFK DYLPKDSLIR IHIVRQIFSV LNSYNFDLID TPVLEYSDLL LKKSGDETEK
QIYRFKDNGG RDVSMRFDLT VPFARFVATN ISALKLPFRR SQFGKVFRGE NSQKGRYREF
MQFDFDIVGE DTFRGDAEIL SVVYYGLEEI FLNFIEGINK KFIIHYSHIG ILNSFFEKLG
LKEKSIFILR NIDKIDKIGI DKVKEALLLE IEKEAVDSIL SLVSLQGTFK DKIQALKSIL
GDNESIKRVE DVFQHLSLLK IQDSFNLNLK ISRGLDYYTG IVFESEVFGS NMGSVCSGGR
YDNLVSSFSN SIQKISGVGG SFGVDRIKDI IDLEKFSYIK IFVTKARSKV LIVNLDSALQ
NYYYELATRF RNHDYSKVKN ISCEVYFKNK NGKNIKEQIE YALSKEIRFL VFVGQEEYKE
NKMKVRDLTK KEELLLSFEE SINLIKCNEK LLCTPF