HISZ_BACC2
ID HISZ_BACC2 Reviewed; 420 AA.
AC B7IN97;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-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};
GN OrderedLocusNames=BCG9842_B3887;
OS Bacillus cereus (strain G9842).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405531;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G9842;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus G9842.";
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; CP001186; ACK94576.1; -; Genomic_DNA.
DR RefSeq; WP_000170302.1; NC_011772.1.
DR AlphaFoldDB; B7IN97; -.
DR SMR; B7IN97; -.
DR EnsemblBacteria; ACK94576; ACK94576; BCG9842_B3887.
DR KEGG; bcg:BCG9842_B3887; -.
DR HOGENOM; CLU_025113_0_0_9; -.
DR OMA; ELVMPPM; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000006744; 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_1000117671"
SQ SEQUENCE 420 AA; 48842 MW; C0A5AF80722AF186 CRC64;
MTKWKRANPN GTRDYLFEEC TLIEEVEQKL RLTFLERGYE EIRTPTIEFY DVFAFQNRPI
DEEKMYKFFD EKGRIIVLRP DMTIPLARVI GTQRWDTPLK VTYSGNVFRA NESHSGKYNE
IVQSGIEVIG IDNVRAEIEC VISVIQALQK LNVQSFTIEI GQVQLYKCIV KKLSIHDEEE
RVLRTYIESK NYAALSNFIG EKKLDRCDET VRLLEKLPRL FGNLEVIEEA EKLASSNEMK
MAIARVKEMY ETMETLGYGS YISIDLGMIQ HLDYYTGVIF KGYIYEIGEE IVSGGRYDEL
IGNFGETLPA VGLAVQVNQI VKALQEQQEP YERNQIDIVI HYELNRLAEA ERLRNLLRKD
GKNAWLSLFS NLSDTFQFAR KNKIGTVVEA KNEYLVEYVW NEKWVVQKEG ETSCVTFKLR