ID   HISZ_HELHP              Reviewed;         280 AA.
AC   Q7VHL1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; OrderedLocusNames=HH_0955;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77552.1; -; Genomic_DNA.
DR   RefSeq; WP_011115795.1; NC_004917.1.
DR   AlphaFoldDB; Q7VHL1; -.
DR   SMR; Q7VHL1; -.
DR   STRING; 235279.HH_0955; -.
DR   EnsemblBacteria; AAP77552; AAP77552; HH_0955.
DR   KEGG; hhe:HH_0955; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_939330_0_0_7; -.
DR   OMA; WFYIQPV; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002495; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/HisZ.
DR   PANTHER; PTHR43707; PTHR43707; 2.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..280
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171037"
SQ   SEQUENCE   280 AA;  32195 MW;  B4ECB80E2BB959A8 CRC64;
     MILEHELPQG SKLYFDMSAR LKRDIESCAI KAFYENDYRE IVTPSFAFLE HQGDMFNREI
     VRLSSENNHQ IGLRYDTTLD AMRIVTKRIM RSSTHKKWFY IQPVFSYPTT EIHQIGAEYL
     GGESLSPVMC LGVSILQTLN LAPYLQISNM KIPFLCAKHS DVDIEVFALQ NVGKLLQMEG
     YMADLVHIKT KQDLQKAILS APAFLKEELE RLLECASYCE YEKTIFSPLL FAPSPYYEDL
     FFRMFVGNST LLQGGKYSVE EQFSCGFAIY TDEVVECLLS