ID   HISZ_BACMK              Reviewed;         420 AA.
AC   A9VLH1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125};
GN   OrderedLocusNames=BcerKBAB4_1326;
OS   Bacillus mycoides (strain KBAB4) (Bacillus weihenstephanensis).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=315730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBAB4;
RX   PubMed=17434157; DOI=10.1016/j.cbi.2007.03.003;
RA   Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C.,
RA   Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V.,
RA   Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "Extending the Bacillus cereus group genomics to putative food-borne
RT   pathogens of different toxicity.";
RL   Chem. Biol. Interact. 171:236-249(2008).
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; CP000903; ABY42573.1; -; Genomic_DNA.
DR   RefSeq; WP_002140970.1; NC_010184.1.
DR   AlphaFoldDB; A9VLH1; -.
DR   SMR; A9VLH1; -.
DR   STRING; 315730.BcerKBAB4_1326; -.
DR   EnsemblBacteria; ABY42573; ABY42573; BcerKBAB4_1326.
DR   GeneID; 66263545; -.
DR   KEGG; bwe:BcerKBAB4_1326; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002154; 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_1000095444"
SQ   SEQUENCE   420 AA;  48820 MW;  A7755A310DE824A4 CRC64;
     MTKWKRANPN GTRDYLFEEC TLIEEVEQKL RRTFLERGYE EIRTPTIEFY DVFAFQNRPI
     DEEKMYKFFD EKGRIIVLRP DMTIPLARVI GTQRGDIPLK VTYSGNVFRA NESLTGKYNE
     IVQSGIEIIG IENVRAEIEC VISVIQALQK LKVQSFTIEI GQVQLYKCIV KKLPINDEEE
     KLLRTYIESK NYAALSHFIE EKKLNRCDET VRLLEKLPRL FGSLDVVEEA EKLASSNEMK
     MAIARVKEIY ETIEQLGYGS YISIDLGMVQ HLDYYTGVIF KGYIYEIGEE IVSGGRYDEL
     IGNFGEMMPA VGLAVQVNQI VKALQEQQEP YKRKRIDIMI HYELNRLAEA ERLRNLLQKD
     GKNAQLSLFS NLNDTFQFAN KNKIMTVVEA KSESLVEYVW REKWIIQKEG EASCVTFKLR