ID   HISZ_NEIM0              Reviewed;         383 AA.
AC   A9M3P6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=NMCC_0778;
OS   Neisseria meningitidis serogroup C (strain 053442).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=374833;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=053442;
RX   PubMed=18031983; DOI=10.1016/j.ygeno.2007.10.004;
RA   Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z.,
RA   Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z.,
RA   Liang X., Xu J., Jin Q.;
RT   "Characterization of ST-4821 complex, a unique Neisseria meningitidis
RT   clone.";
RL   Genomics 91:78-87(2008).
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; CP000381; ABX72971.1; -; Genomic_DNA.
DR   RefSeq; WP_002251231.1; NC_010120.1.
DR   AlphaFoldDB; A9M3P6; -.
DR   SMR; A9M3P6; -.
DR   EnsemblBacteria; ABX72971; ABX72971; NMCC_0778.
DR   KEGG; nmn:NMCC_0778; -.
DR   HOGENOM; CLU_025113_0_1_4; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001177; 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.
FT   CHAIN           1..383
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000076248"
SQ   SEQUENCE   383 AA;  41765 MW;  8D8A3F1A85B241F2 CRC64;
     MQTWQLPEHI ADVLPTNARQ LESAREQLLA LFRVHGYELV QPPLMEYAHS LLTHIDAGLS
     LKTILVTDRL SGRQLGIRAD ITPQVARIDA HLLSANQGIN RLCYAGPVLH AQPDGLLNMR
     EPLQAGAEMY GFADIRGDIE LIDLMLKSMK IADMGKVLLS LGHIGIFRAL SDAAHLDAGQ
     SATLLALMQD KDTGAVEAQV KAWKLDGMWA KAFSLLPRLY GGREVLSDAR GRLPDLSAVG
     GALGELQAVC DAFPDCEIHI DLSELRVDNY HTGLLYAAYA ADFHDAVARG GRYDGLGGYF
     GRARPATGFS FDLRSFIGRL PAIERQPAVL VDAEDAEAAR EAVEALREQG QCVVIDYGIG
     HNVSEELAGR LKKTDGVWQV VKR