ID HISZ_BACC3 Reviewed; 420 AA.
AC C1EMB3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=BCA_1459;
OS Bacillus cereus (strain 03BB102).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=572264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=03BB102;
RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C.,
RA Tapia R., Han C., Sutton G., Sims D.;
RT "Genome sequence of Bacillus cereus 03BB102.";
RL Submitted (FEB-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001407; ACO27689.1; -; Genomic_DNA.
DR RefSeq; WP_000170325.1; NZ_CP009318.1.
DR AlphaFoldDB; C1EMB3; -.
DR SMR; C1EMB3; -.
DR KEGG; bcx:BCA_1459; -.
DR PATRIC; fig|572264.18.peg.1409; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000002210; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 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 NCBIfam; TIGR00443; hisZ_biosyn_reg; 1.
DR PANTHER; PTHR43707:SF6; ATP PHOSPHORIBOSYLTRANSFERASE REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 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_1000122662"
SQ SEQUENCE 420 AA; 48784 MW; C23502F68DAB40C2 CRC64;
MTKWKRANPN GTRDYLFEEC TLIEEVEQKL RRTFLERGYE EIRTPTIEFY DVFAFQSRPI
DEEKMYKFFD EKGRIIVLRP DMTIPLARVV GTQRCDTPLK VTYSGNVFRA NESLAGKYNE
IVQSGIEVIG IDNVRAEIEC VISVIQSLQK LKVQSFTIEI GQVQLYKCIV KKLSIHEEEE
KVLRTYIESK NYASLSNFIR DKKLDRCDET VKLLEKLPRL FGNLEVIEEA EKLASSNEMK
MAITRVKEIY EAIEKLGYGS YISIDLGMIQ HLDYYTGVIF KGYIYEIGEE IVSGGRYDEL
IGNFGEMLPA VGLAVQVNQI VKALQEQQEP YERKRIDIMI HYELNRLAEA ERLRNLLQKD
GKKVALSLFS NLNDTFQFAR KNQIVTVVEA KSESLVEYVW KEKWVVQKEG ETSCVTFKLR
//
