SYH_MYCPN
ID SYH_MYCPN Reviewed; 414 AA.
AC P75069;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=MPN_045; ORFNames=MP109;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 29342 / M129;
RX PubMed=11271496;
RX DOI=10.1002/1522-2683(200011)21:17<3765::aid-elps3765>3.0.co;2-6;
RA Regula J.T., Ueberle B., Boguth G., Goerg A., Schnoelzer M., Herrmann R.,
RA Frank R.;
RT "Towards a two-dimensional proteome map of Mycoplasma pneumoniae.";
RL Electrophoresis 21:3765-3780(2000).
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; U00089; AAB95757.1; -; Genomic_DNA.
DR PIR; S73435; S73435.
DR RefSeq; NP_109733.1; NC_000912.1.
DR RefSeq; WP_010874402.1; NC_000912.1.
DR AlphaFoldDB; P75069; -.
DR SMR; P75069; -.
DR STRING; 272634.MPN_045; -.
DR EnsemblBacteria; AAB95757; AAB95757; MPN_045.
DR GeneID; 66609317; -.
DR KEGG; mpn:MPN_045; -.
DR PATRIC; fig|272634.6.peg.45; -.
DR HOGENOM; CLU_025113_1_1_14; -.
DR OMA; CDFDFIG; -.
DR BioCyc; MPNE272634:G1GJ3-62-MON; -.
DR BRENDA; 6.1.1.21; 3534.
DR Proteomes; UP000000808; 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 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 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 CHAIN 1..414
FT /note="Histidine--tRNA ligase"
FT /id="PRO_0000136205"
SQ SEQUENCE 414 AA; 47262 MW; 6FFC3C5F4C92B2D5 CRC64;
MSVLQKPRGV KDWYGEELIY FNWTVHQITN LAWKWGFSEV KTPLLEYAEA FKRTNANADI
VKKELYEFHD KSNRLLALRP EATAGIVRLV CENKLLQPQN YPLRLFTIGT MYRYERPQSN
RYREHYQFSC EVIGDTNPTV LLDTLLLGHA IIQQLGIEGV ILKLNNLGNS ATIQQWNQAL
QAYLTQFKAQ LTELSQSRLS TNPLRILDDK VDGQLPFISD APQIEQFLDA EQQALNTWLQ
QQLTQQQVPF EWNPTLVRGL DYYTGVVFEF VKDDTTVLAG GVYDNLVEEL GGTPTKALGF
ACGIERSINC LSAVKKQAIL ANQPPRLLVI GLTEAALEKL LQLSLGWRAY HPVTIYPKVI
RIINGIRAAQ RLGYRFLGVI GGNNLEQQTI TVKDLATEQQ TTYTWDEFRQ RQVL