ID   HISZ_STAA8              Reviewed;         272 AA.
AC   Q2FUT6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, 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};
GN   OrderedLocusNames=SAOUHSC_03015;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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; CP000253; ABD32001.1; -; Genomic_DNA.
DR   RefSeq; WP_001065590.1; NZ_LS483365.1.
DR   RefSeq; YP_501464.1; NC_007795.1.
DR   AlphaFoldDB; Q2FUT6; -.
DR   SMR; Q2FUT6; -.
DR   STRING; 1280.SAXN108_2954; -.
DR   EnsemblBacteria; ABD32001; ABD32001; SAOUHSC_03015.
DR   GeneID; 3921496; -.
DR   KEGG; sao:SAOUHSC_03015; -.
DR   PATRIC; fig|93061.5.peg.2723; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_089652_0_0_9; -.
DR   OMA; RYYSNYP; -.
DR   UniPathway; UPA00031; UER00006.
DR   PRO; PR:Q2FUT6; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_00125; HisZ; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004517; HisZ.
DR   Pfam; PF13393; tRNA-synt_His; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..272
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000016286"
SQ   SEQUENCE   272 AA;  31681 MW;  B69B2019A8D88C26 CRC64;
     MNNSEQLIAL KESETAFLKY FNKADYELVD FSVVEKLDWK QLNHEDLQQM GERNFWQHEH
     QIYALRNDFT DQLLRYYSMY PTAATKVAYT GLIIRNNEAA VQVGLENYAP SLANVQQSLK
     LFIQFIQQQL RDNVHFVVLG HYQLLDALLD KSLQTPDILS MIEERNLSGL VTYLSTEHPI
     VQILKENTQQ QLNVLEHYIP NDHPALVELK IWERWLHKQG YKDIHLDITA QPPRSYYTGL
     FIQCHFAENE SRVLTGGYYK GSIEGFGLGL TL