ID   HISZ_THET2              Reviewed;         361 AA.
AC   P62360;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=TT_C1865;
OS   Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=262724;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-163 / DSM 7039 / HB27;
RX   PubMed=15064768; DOI=10.1038/nbt956;
RA   Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H.,
RA   Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C.,
RA   Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P.,
RA   Kramer W., Merkl R., Gottschalk G., Fritz H.-J.;
RT   "The genome sequence of the extreme thermophile Thermus thermophilus.";
RL   Nat. Biotechnol. 22:547-553(2004).
CC   -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC       allow the feedback regulation of ATP phosphoribosyltransferase activity
CC       by histidine. {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC       {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00125}.
CC   -!- MISCELLANEOUS: This function is generally fulfilled by the C-terminal
CC       part of HisG, which is missing in some bacteria such as this one.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       HisZ subfamily. {ECO:0000255|HAMAP-Rule:MF_00125}.
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DR   EMBL; AE017221; AAS82207.1; -; Genomic_DNA.
DR   RefSeq; WP_011174219.1; NC_005835.1.
DR   AlphaFoldDB; P62360; -.
DR   SMR; P62360; -.
DR   STRING; 262724.TT_C1865; -.
DR   PRIDE; P62360; -.
DR   EnsemblBacteria; AAS82207; AAS82207; TT_C1865.
DR   GeneID; 3168065; -.
DR   KEGG; tth:TT_C1865; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_0; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000592; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00125; HisZ; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   InterPro; IPR004517; HisZ.
DR   PANTHER; PTHR43707; PTHR43707; 1.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT   CHAIN           1..361
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171073"
SQ   SEQUENCE   361 AA;  40053 MW;  2262A61A683F1C40 CRC64;
     MIPEGTRFLL PPEARLKAEV VGKLQHLFRR HGYEPVELPA LELYDPDHPL AERAFKLVDK
     TGEVLALRSE FTTLLAKLLR AHLGEGAHRF QYAGPLWLRE ADAELGRLRE YTQVGLELLG
     ATGPLADAEV LELAFAALEA LGVQGEVEVG LPSLVGEVLK ASGLPEALQR RAQQAIHRKN
     LPELKGLLAE SPVPEEARKV LLALPDLYGG REVLKEARGL PLPPKAQEAL AQLERTLDLL
     GRPVLLDLGM ARRYEYYSGI FFRAYTPGFG LPLLGGGRYD GALFPKAAGF ALGVERLLEA
     LRLPKEEEPP EVLALDLKAL RRFARERRTE LFHGEDPVAY ARRRGIPFLA RGEELFRVEE
     A