ID   HISZ_SYMTH              Reviewed;         399 AA.
AC   Q67KH4;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; Synonyms=hisS2;
GN   OrderedLocusNames=STH2839;
OS   Symbiobacterium thermophilum (strain T / IAM 14863).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=292459;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T / IAM 14863;
RX   PubMed=15383646; DOI=10.1093/nar/gkh830;
RA   Ueda K., Yamashita A., Ishikawa J., Shimada M., Watsuji T., Morimura K.,
RA   Ikeda H., Hattori M., Beppu T.;
RT   "Genome sequence of Symbiobacterium thermophilum, an uncultivable bacterium
RT   that depends on microbial commensalism.";
RL   Nucleic Acids Res. 32:4937-4944(2004).
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; AP006840; BAD41824.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q67KH4; -.
DR   SMR; Q67KH4; -.
DR   STRING; 292459.STH2839; -.
DR   EnsemblBacteria; BAD41824; BAD41824; STH2839.
DR   KEGG; sth:STH2839; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000417; 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;
KW   Reference proteome.
FT   CHAIN           1..399
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000242860"
SQ   SEQUENCE   399 AA;  42441 MW;  0372C1233169CC92 CRC64;
     MSTPVTRTQV PDGVRDRLPS EAAAMRRLSA RLDNVFRAWG YREVSTPVIE YLEAVAAGAA
     NWGRREDLYQ FFDRKGRTLA LRPDMTTPIA RLMATRLADE PLPLRLSYFA PVFRHRELRA
     GATSEIWQAG VELVGAPGEA ADAEVISLAC AAVRAADLTG FRIGLGHVGV VEGLFESAGV
     DPQAAAVLKE AMVARDLVAF EQGVARAGLS GERAERLLAL VHFHGSYAEA VARFGGVGGR
     VAEALQHLGR VLEVLEALGV AEQVNLDLGL VRSLGYYTGV VFEGYLPGIG APVLGGGRYD
     NLVAEFGRPL AATGFALEVD RLLMAQEQQG ALAAEPGLDA VIACPPGQEA AAMAWAARLR
     AQGLAVEVDF LDRTGEELAA YARARAAARV LRPGVPSIH