ID   HISZ_CLOB6              Reviewed;         422 AA.
AC   C3KVW9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=CLJ_B1672;
OS   Clostridium botulinum (strain 657 / Type Ba4).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=515621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=657 / Type Ba4;
RA   Shrivastava S., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A.,
RA   Smith T.J., Sutton G., Brettin T.S.;
RT   "Genome sequence of Clostridium botulinum Ba4 strain 657.";
RL   Submitted (MAY-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; CP001083; ACQ52482.1; -; Genomic_DNA.
DR   RefSeq; WP_012720670.1; NC_012658.1.
DR   AlphaFoldDB; C3KVW9; -.
DR   SMR; C3KVW9; -.
DR   EnsemblBacteria; ACQ52482; ACQ52482; CLJ_B1672.
DR   KEGG; cbi:CLJ_B1672; -.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002333; 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_1000203113"
SQ   SEQUENCE   422 AA;  48629 MW;  1897564453D26076 CRC64;
     MGNWNKYIPK GMKDILFEES NIKLDIEDQL RKIYKYSGFS EIISPTIEFY DVFNSNIQAI
     PQEKMYKLFD NLGRILVLRP DMTTPIGRIT GTKMKDCTYP LKLCYTANIF RVNEKLNGKR
     GEITQSGIEI IGTKGIKSDV DSIVTAINAL LSLGLRNFKI ELGEAGLFEA LTENMRIEEE
     NLKKLKEIIR NKNYVALKKF LDEISLKYSK EDFEIIENLP KLFGDIEIIE KAKALTKNEK
     ALKSLNDIYN IYKSIEDIGL GSYISIDLGM VQNIDYYTGV IFKGYVEEVG DSILSGGRYD
     NLIQHFGIEL PATGFAINVD DIMIALKKQN TMSMDKDKKV LIFYKEEFLR KAYDFMQELK
     MKKIICELSL LDEDKEILLY SKKKGIDFII GFTREEKLFV KDLKSDKIAF LEKNEIEDLL
     MV