ID   HISZ_HERAR              Reviewed;         383 AA.
AC   A4G4L1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=HEAR1274;
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1;
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier P., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.-C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL61448.2; -; Genomic_DNA.
DR   RefSeq; WP_041322244.1; NC_009138.1.
DR   AlphaFoldDB; A4G4L1; -.
DR   SMR; A4G4L1; -.
DR   STRING; 204773.HEAR1274; -.
DR   EnsemblBacteria; CAL61448; CAL61448; HEAR1274.
DR   KEGG; har:HEAR1274; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_1_4; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000006697; 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; 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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..383
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000095459"
SQ   SEQUENCE   383 AA;  41882 MW;  19A1C98BE8DCBAE5 CRC64;
     MPNWLLPENI ADVLPSEARK IEELRRLIID NFHLYGYELV MPPMLEYLES LLAGAGHDMD
     LRTFKLIDQL SGRTLGVRAD MTTQVARIDA HLLNRASITR LCYCGSVLQT RPNGLHATRE
     PLQIGAEVYG HGGLEADAEI QELALASLAL AGFTQVRIDL CHVGVLRAII ASDVQAQKDE
     NALYTFLRAK DVPALQEMTL TYGADTRRAL LALPGLYGDV TVIARAREIL PKLPGIDTAL
     DELIALAGLA GETSVTIDLA DLGGYQYESG VMFAIYVPGL PNAVARGGRY DHVGEAFGRA
     RPATGFSMDL RELARLLPDA EPKLAIRAPW GREPALRTKI GALRKAGEIV IQSLSGHEND
     QDEFECDRVL VLEDGNWIIK NLG