ID   HISZ_NEIMB              Reviewed;         383 AA.
AC   Q9K013;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; OrderedLocusNames=NMB0814;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(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; AE002098; AAF41227.1; -; Genomic_DNA.
DR   PIR; E81156; E81156.
DR   RefSeq; NP_273856.1; NC_003112.2.
DR   RefSeq; WP_002213944.1; NC_003112.2.
DR   AlphaFoldDB; Q9K013; -.
DR   SMR; Q9K013; -.
DR   STRING; 122586.NMB0814; -.
DR   PaxDb; Q9K013; -.
DR   EnsemblBacteria; AAF41227; AAF41227; NMB0814.
DR   KEGG; nme:NMB0814; -.
DR   PATRIC; fig|122586.8.peg.1026; -.
DR   HOGENOM; CLU_025113_0_1_4; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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_0000171046"
SQ   SEQUENCE   383 AA;  41746 MW;  8D8A3F07B94193F2 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 VDAEDAEAAH EAVEALREQG QCVVIDYGIG
     HNVSEELAGR LKKTDGVWQV VKR