ID   SYH_CUTAK               Reviewed;         454 AA.
AC   Q6A8J7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 119.
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=PPA1169;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Cutibacterium.
OX   NCBI_TaxID=267747;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16379 / KPA171202;
RX   PubMed=15286373; DOI=10.1126/science.1100330;
RA   Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA   Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT   "The complete genome sequence of Propionibacterium acnes, a commensal of
RT   human skin.";
RL   Science 305:671-673(2004).
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; AE017283; AAT82918.1; -; Genomic_DNA.
DR   RefSeq; WP_002517998.1; NZ_CP025935.1.
DR   AlphaFoldDB; Q6A8J7; -.
DR   SMR; Q6A8J7; -.
DR   STRING; 267747.PPA1169; -.
DR   EnsemblBacteria; AAT82918; AAT82918; PPA1169.
DR   KEGG; pac:PPA1169; -.
DR   PATRIC; fig|267747.3.peg.1205; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_3_0_11; -.
DR   OMA; YQIQKVW; -.
DR   Proteomes; UP000000603; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IEA:InterPro.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 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   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.
FT   CHAIN           1..454
FT                   /note="Histidine--tRNA ligase"
FT                   /id="PRO_0000136224"
FT   REGION          434..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   454 AA;  50276 MW;  5789CC2ED7796BFD CRC64;
     MARLKPLSGF PEFLPSGQMV ENHVTRILEE TFELHGFAPI RTRAVEPMEQ LTRKGEIDKE
     VYVVDRLHAD PHDTRSGKDR LGLHFDLTVP FARYVLENAG HLYFPFRRYQ IQKVWRGERP
     QEGRYREFTQ ADIDIVGDQT LAEHHDVETP LVMLSALERL HTELGFPTVT MHVNNRKLSE
     GFYRGLGIAD PMAVLQRVDK YDKIGPDAVR KLLVDELNLS DDAAAKCVAL ASIQSTDDSF
     IAKVRELGVA NDMLEEGLDS LNRVVAAVNK AVPGRMVANL KIARGLDYYT GTVYETELTG
     HESMGSVCSG GRYESLASDG KHVYPGVGIS LGLTRLLAPI LSRGELSSSR SVPSAVLVAV
     NTEEDRATSE VIASALRSRG IPCEVAPKAD KFGKQIKHAD RRGIPFVWFP GVKHADYRDA
     DTVKDIRSGD QVEADAGAWN PPTEDLHPGV IGTW