SYH_TREPS
ID SYH_TREPS Reviewed; 442 AA.
AC B2S3N0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 73.
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}; OrderedLocusNames=TPASS_0641;
OS Treponema pallidum subsp. pallidum (strain SS14).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=455434;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SS14;
RX PubMed=18482458; DOI=10.1186/1471-2180-8-76;
RA Matejkova P., Strouhal M., Smajs D., Norris S.J., Palzkill T.,
RA Petrosino J.F., Sodergren E., Norton J.E., Singh J., Richmond T.A.,
RA Molla M.N., Albert T.J., Weinstock G.M.;
RT "Complete genome sequence of Treponema pallidum ssp. pallidum strain SS14
RT determined with oligonucleotide arrays.";
RL BMC Microbiol. 8:76-76(2008).
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; CP000805; ACD71059.1; -; Genomic_DNA.
DR RefSeq; WP_010882086.1; NC_021508.1.
DR AlphaFoldDB; B2S3N0; -.
DR SMR; B2S3N0; -.
DR PRIDE; B2S3N0; -.
DR EnsemblBacteria; ACD71059; ACD71059; TPASS_0641.
DR GeneID; 57879166; -.
DR KEGG; tpp:TPASS_0641; -.
DR PATRIC; fig|455434.6.peg.635; -.
DR OMA; YQIQKVW; -.
DR Proteomes; UP000001202; 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 Gene3D; 3.30.930.10; -; 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; IPR015807; His-tRNA-ligase.
DR InterPro; IPR041715; HisRS-like_core.
DR InterPro; IPR004516; HisRS/HisZ.
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.
FT CHAIN 1..442
FT /note="Histidine--tRNA ligase"
FT /id="PRO_1000095608"
SQ SEQUENCE 442 AA; 50199 MW; 079E2F89784D632B CRC64;
MRVGSAVSPK VLKGFRDLLP DEEIERALLV EKLTVALRQM GFVPIDTPAL EYTEVLLRKS
EGDTEKQMFR FVDKGGRDVA LRFDLTVPLA RFVATHYARL YFPFKRYHFA KVWRGEKPQM
GRYREFTQCD FDIVGSDSVC ADFEILKSIR HMLYMAGAEH IRIHVAHRGL FDRFLRALSL
SDQAEHILRI IDKRAKMAPH VLTAQLESLC DPVRVQKIMT YVSAGEVDGV APSFEHTLSA
IETLTGGVSE ESTRLRKIYE LLCAVNIQSS YVFDPSITRG FDYYTGMVCE TFLTQLPHIG
SVCSGGRYDH LTALYMKDAV SGVGASIGLD RLYAAFQQLG MSREHVCFVQ ALIFCQDSAL
MDVYQKLCSY FAVQVATEVF PDPRKLSQQY AFAEKKGIRW GIFVEQRNAV VEDCLLVLRD
LSTRKDTRLP AHEVRRRMAA EG
