ID   HISZ_ALKCK              Reviewed;         393 AA.
AC   Q5WDH6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=ABC3050;
OS   Alkalihalobacillus clausii (strain KSM-K16) (Bacillus clausii).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=66692;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KSM-K16;
RA   Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y.,
RA   Kawai S., Ito S., Horikoshi K.;
RT   "The complete genome sequence of the alkaliphilic Bacillus clausii KSM-
RT   K16.";
RL   Submitted (OCT-2003) 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; AP006627; BAD65584.1; -; Genomic_DNA.
DR   RefSeq; WP_011247892.1; NC_006582.1.
DR   AlphaFoldDB; Q5WDH6; -.
DR   SMR; Q5WDH6; -.
DR   STRING; 66692.ABC3050; -.
DR   EnsemblBacteria; BAD65584; BAD65584; ABC3050.
DR   KEGG; bcl:ABC3050; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; HQCDFDI; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001168; 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;
KW   Reference proteome.
FT   CHAIN           1..393
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000242820"
SQ   SEQUENCE   393 AA;  44277 MW;  510990F99295B602 CRC64;
     MSEPFMFEKP LGMRDVLPNL HSMQRKLGDR VLQEFRLWGY EQVQTPTLEY YETVGKASAI
     SDKQLFKLID FHGNTLVLRP DMTAPIARLV SSSMKDIPYP LRLSYCSSLY RALQTEGGRP
     AEFAQVGVEL VGDHTASADG EMLLLLNRAL IQAGLDHFQV AVGHIGFLNA LFLEIFGTVE
     RAELLRRQLY EKNDVGFKEQ VKAFGLSSID EKKLLKLSRL RGNEAILAEA EQLTESAEGK
     QAVAELRDLW QGLKEGGLTR YMKLDLSLVL HMSYYTGCIF EVYHDRLPRP LGGGGRYDHL
     LAKFGRPGPA TGFGLRLDLL AEAVGKLEVQ PKKRCLLYSR ERRQEAYRKA TALREKGMQV
     VLQDVAGVDD IDKMSASYEE IVYLIGKTEE GKR