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Database: UniProt
Entry: P75069
LinkDB: P75069
Original site: P75069 
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   27-MAR-2024, entry version 129.
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 / Subtype 1)
OS   (Mycoplasmoides pneumoniae).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
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 / Subtype 1;
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; NZ_OU342337.1.
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   OrthoDB; 9800814at2; -.
DR   BioCyc; MPNE272634:G1GJ3-62-MONOMER; -.
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; 3.40.50.800; Anticodon-binding domain; 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   NCBIfam; TIGR00442; hisS; 1.
DR   PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR   SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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
//
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