ID   HISZ_GEOSW              Reviewed;         392 AA.
AC   C5D7P4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=GWCH70_2981;
OS   Geobacillus sp. (strain WCH70).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=471223;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WCH70;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brumm P., Mead D.A., Richardson P.;
RT   "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL   Submitted (JUN-2009) 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; CP001638; ACS25654.1; -; Genomic_DNA.
DR   RefSeq; WP_015865042.1; NC_012793.1.
DR   AlphaFoldDB; C5D7P4; -.
DR   SMR; C5D7P4; -.
DR   STRING; 471223.GWCH70_2981; -.
DR   EnsemblBacteria; ACS25654; ACS25654; GWCH70_2981.
DR   KEGG; gwc:GWCH70_2981; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
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..392
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000203114"
SQ   SEQUENCE   392 AA;  44570 MW;  D771C16797668DA1 CRC64;
     MTKKLFMFEK PLGMRDTLPF LYEIKKRVRQ AMIREIETWG YELIETPTLE YYETVGTVSA
     IDDHQLFKLL DQQGHTLVLR PDMTAPIARL AASRLYKEGN PLRLAYNANV FRAQQREGGR
     PAEFEQIGVE CIGDGTVAAD AEVISVMIAA LRQAGLQHFT VTIGHIGYVN ALFLEIVGNE
     ERASVLRRFL YEKNYVGYRE HVKSLPLSSI DQKRLLQLLH LHGNDMTMEE AKELVHSEEG
     KRAVDDLCEL SNALQLYGVD DVVKIDMTLV SHMSYYTGIL FEVYAEHVGF PIGNGGRYDE
     LLEKFSRKAP ATGFGIRVDR LIEALGESEE EAAIECIVFS QERFAEAIEL ARTKRREGKR
     VVLQHISGIR DIDAYSKRYK PITYLLGSTE KE