ID   HISZ_STAAM              Reviewed;         272 AA.
AC   P64379; Q99QW1;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; OrderedLocusNames=SAV2680;
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
CC   -!- FUNCTION: Required for the first step of histidine biosynthesis. May
CC       allow the feedback regulation of ATP phosphoribosyltransferase activity
CC       by histidine (By similarity). {ECO:0000250}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC       from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9.
CC   -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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:0000305}.
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DR   EMBL; BA000017; BAB58842.1; -; Genomic_DNA.
DR   RefSeq; WP_001065591.1; NC_002758.2.
DR   AlphaFoldDB; P64379; -.
DR   SMR; P64379; -.
DR   PaxDb; P64379; -.
DR   EnsemblBacteria; BAB58842; BAB58842; SAV2680.
DR   KEGG; sav:SAV2680; -.
DR   HOGENOM; CLU_089652_0_0_9; -.
DR   OMA; RYYSNYP; -.
DR   BioCyc; SAUR158878:SAV_RS14630-MON; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002481; 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.
FT   CHAIN           1..272
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171060"
SQ   SEQUENCE   272 AA;  31654 MW;  E6843F19A8D89B2D CRC64;
     MNNSEQLIAL KESETAFLKY FNKADYELVD FSVVEKLDWK QLNHEDLQQM GERNFWQHEH
     QIYALRNDFT DQLLRYYSMY PTAATKVAYT GLIIRNNEAA VQVGLENYAP SLANVQQSLK
     LFIQFIQQQL RDNVHFVVLG HYQLLDALLD KSLQTPDILS MIEERNLSGL VTYLSTEHPI
     VQILKENTQQ QLNVLEHYIP NDHPALVELK IWERWLHTQG YKDIHLDITA QPPRSYYTGL
     FIQCHFAENE SRVLTGGYYK GSIEGFGLGL TL