ID   HISZ_BACC0              Reviewed;         420 AA.
AC   B7JFY9;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125};
GN   OrderedLocusNames=BCAH820_1495;
OS   Bacillus cereus (strain AH820).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405535;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AH820;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus AH820.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001283; ACK90051.1; -; Genomic_DNA.
DR   RefSeq; WP_000170324.1; NC_011773.1.
DR   AlphaFoldDB; B7JFY9; -.
DR   SMR; B7JFY9; -.
DR   EnsemblBacteria; ACK90051; ACK90051; BCAH820_1495.
DR   KEGG; bcu:BCAH820_1495; -.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001363; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00773; HisRS-like_core; 1.
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   TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT   CHAIN           1..420
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000117670"
SQ   SEQUENCE   420 AA;  48818 MW;  CCD50C186DAB40C8 CRC64;
     MTKWKRANPN GTRDYLFEEC TLIEEVEQKL RRTFLERGYE EIRTPTIEFY DVFAFQSRPI
     DEEKMYKFFD EKGRIIVLRP DMTIPLARVV GTQRCDTPLK VTYSGNVFRA NESLAGKYNE
     IVQSGIEVIG IDNVRAEIEC VISVIQSLQK LKVQSFTIEI GQVQLYKCIV KKLSIHEEEE
     KVLRTYIESK NYASLSNFIR DKKLDRCDET VKLLEKLPRL FGNLEVIEEA EKLASSNEMK
     MAITRVKEIY EAIEKLGYGS YISIDLGMIQ HLDYYTGVIF KGYIYEIGEE IVSGGRYDEL
     IGNFGEMLPA VGLAVQVNQI VKALQEQQEP YERKRIDIMI HYELNRLAEA ERLRNLFQKD
     GKKVALSLFS NLNDTFQFAR KNQIVTVVEA KSESLVEYVW KEKWVVQKEG ETSCVTFKLR