ID   HISZ_AQUAE              Reviewed;         383 AA.
AC   O67223;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; Synonyms=hisS2; OrderedLocusNames=aq_1155;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC       allow the feedback regulation of ATP phosphoribosyltransferase activity
CC       by histidine (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000305}.
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DR   EMBL; AE000657; AAC07188.1; -; Genomic_DNA.
DR   PIR; D70399; D70399.
DR   RefSeq; NP_213787.1; NC_000918.1.
DR   RefSeq; WP_010880725.1; NC_000918.1.
DR   AlphaFoldDB; O67223; -.
DR   SMR; O67223; -.
DR   STRING; 224324.aq_1155; -.
DR   EnsemblBacteria; AAC07188; AAC07188; aq_1155.
DR   KEGG; aae:aq_1155; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_0; -.
DR   InParanoid; O67223; -.
DR   OMA; IFEVYSP; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00773; HisRS-like_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00125; HisZ; 1.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..383
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171021"
SQ   SEQUENCE   383 AA;  44349 MW;  E3B449B58EF86C8D CRC64;
     MKTSLISGER FYSLEESNLV KEIFKKAVKI FEAFGYDYIN LSHFEPYEFQ ELTFGEGSKE
     AITFKDSYTK ESFGLRLDFT TQVVRTISHL RNVKLPERVY YFGKVFSLDR RGFEKLQTGV
     ELIGEKSILA DFEVIQVLTE FLKSLGLKDL KVILSHAGIV RKVADEREEL LRAFSERNLE
     ALKEVLGNDI KFFVEVSKNP EVLNFLEKYD LEKEKEELLE LGKLLEEFGI DYAYDLGEVR
     NFPYYTGVIF EIYELKSGKA LAGGGRYDNL SKIYGKEYPA TGGAVYLERL LDILPKNVEK
     KDYFVIDKTK KRLGLKLADV LREKGKKVGM EIVKERGLEH SLIYAFDKGF KEVLLVEDEI
     VKVYTTPKDY VVMKIREFLD LIE