ID   HISZ_HAHCH              Reviewed;         400 AA.
AC   Q2SBC7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=HCH_05378;
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396;
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABC32047.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000155; ABC32047.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041599905.1; NC_007645.1.
DR   AlphaFoldDB; Q2SBC7; -.
DR   SMR; Q2SBC7; -.
DR   STRING; 349521.HCH_05378; -.
DR   EnsemblBacteria; ABC32047; ABC32047; HCH_05378.
DR   KEGG; hch:HCH_05378; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_1_6; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000238; 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.
DR   TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..400
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000242838"
SQ   SEQUENCE   400 AA;  45048 MW;  B977AD98B7739C6B CRC64;
     MSESDLWLLP DGVEELLPPE ATRIEELRRQ LLDLYHSWGY EMIVPPLLEF LDSLLIGVGR
     DLELEMFKVT DQLTGRLMGI RADMTPQVAR IDSRRSHDVA SRFCYIGSVL RTKSPSMFSS
     RTPIQTGCEL YGVVGSAADI EIISLMLETL NLAKISPLHM DIAHVGVYQA ILAEAKLSKI
     QSEELFEALR RKAIPEVDEI AATIPDKAIR QKVMALPRLA GGKEKMKEAR KIFAGNPDIE
     YALDEMSQVA AVIGERYPEV EIYFDFCEMR GYKYYTGLVF AAYTEGLGQA VAKGGRYDEV
     GRDFGRGRPA MGFSVDLKAL YRMGKREWAQ PAGAILAPNG QDAELWELIR QLRRSNRVIQ
     LMPGEEAGHW ASHCDRQIVR DESGQWIVKP LTEFNPNHVK