ID   HISZ_CLOBJ              Reviewed;         422 AA.
AC   C1FN35;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   25-MAY-2022, entry version 66.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=CLM_1806;
OS   Clostridium botulinum (strain Kyoto / Type A2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=536232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Kyoto / Type A2;
RA   Shrivastava S., Brinkac L.M., Brown J.L., Bruce D., Detter C.C.,
RA   Johnson E.A., Munk C.A., Smith L.A., Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum A2 Kyoto.";
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; CP001581; ACO86208.1; -; Genomic_DNA.
DR   RefSeq; WP_012705189.1; NC_012563.1.
DR   AlphaFoldDB; C1FN35; -.
DR   SMR; C1FN35; -.
DR   STRING; 536232.CLM_1806; -.
DR   EnsemblBacteria; ACO86208; ACO86208; CLM_1806.
DR   KEGG; cby:CLM_1806; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001374; 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..422
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000122665"
SQ   SEQUENCE   422 AA;  48580 MW;  A8B8785F475332FC CRC64;
     MENWNKYIPE GMKDILFKES NIKLNIEDQL RKIYKYSGFS EIISPTIEFY DVFNSNIQAI
     PQEKMYKLFD NLGRILVLRP DMTTPIGRIT GTKMKDCTYP LKLCYTANIF RVNEKLNGKR
     GEITQSGIEI IGTNGIKSDV DSIVTAINAL LSVGLKNFKI ELGEAGFFQA LTENMEIKEE
     NLKKLKEIIR NKNYVALKKF LDEISSKYSK EDFELIKNLP KLFGDIKIIE KAKALTKNKK
     ALKSLDDIHN IYKSIENIGL EAYISIDLGM VQNIDYYTGV IFKGYVEEVG DSILSGGRYD
     NLIQHFGIEL PATGFAINVD DIMIALKKQN TMSMDKDKKV LIFYKEEFLR KAYDFMQELK
     MKKIICELSL LDDDKEILLY SKKKGIDFII GFMGEEKLFV KDLKSDKIAF LKKDEIENLL
     ML