ID   HISZ_RHILO              Reviewed;         373 AA.
AC   Q987S9;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; OrderedLocusNames=mlr6929;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB53121.1; -; Genomic_DNA.
DR   RefSeq; WP_010914431.1; NC_002678.2.
DR   AlphaFoldDB; Q987S9; -.
DR   SMR; Q987S9; -.
DR   STRING; 266835.14026524; -.
DR   EnsemblBacteria; BAB53121; BAB53121; BAB53121.
DR   KEGG; mlo:mlr6929; -.
DR   PATRIC; fig|266835.9.peg.5512; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_6_0_5; -.
DR   OMA; YYTGFEF; -.
DR   OrthoDB; 277998at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000552; 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; 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.
FT   CHAIN           1..373
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171057"
SQ   SEQUENCE   373 AA;  39622 MW;  963B5ED0AE420811 CRC64;
     MTSRFPAIAA NITKLFAARN THAVEVAILQ PADPFLDMAG EDLRRRIFLT ESETGQTLCL
     RPEFTIPVCL DHISSQAGTP RRYSYLGEVF RQRREGGNEF FQAGIEDLGD RDTAQADARS
     VADAHALLSL VLPGRSLAVT LGDQGIFEAV LAALGLPRGW RMRLARAFGS APMLQAALAD
     LANPPRNGQL SGEVAALVLD GDLDGLSTHI AGGMEQAGLS ASAGRSPTDI ARRLIEKAEL
     RSVRLSNEAF AALKNFLAIH VPLDGAARAL ETFAAGAGLS LGAALEKFAA RAKAIEAHGL
     PAEKIRYDAA FGRPLDYYTG VVFEIAAQGG ERPLAGGGRY DRLLTLLGAK TAIPGVGFSV
     WLDRIEALRE AAP