ID   HISZ_PROM4              Reviewed;         392 AA.
AC   A9BAD0;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=P9211_08611;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA   Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA   Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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; CP000878; ABX08792.1; -; Genomic_DNA.
DR   RefSeq; WP_012195414.1; NC_009976.1.
DR   AlphaFoldDB; A9BAD0; -.
DR   SMR; A9BAD0; -.
DR   STRING; 93059.P9211_08611; -.
DR   EnsemblBacteria; ABX08792; ABX08792; P9211_08611.
DR   KEGG; pmj:P9211_08611; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_3; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000788; 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..392
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000095466"
SQ   SEQUENCE   392 AA;  44525 MW;  CC6FB8FB4752C132 CRC64;
     MAKQSTLGSK ELNPRQVEEN NLLATKLSEI YKKWGYQEVA PPQVEGLKTL MAGGGIDSKE
     ILKLVIDEPV GLRPEMTASI ARAASTRYVA EPRPLRLWAS GTIFKSREES DGKIVIDESL
     QSGVELFGIE GMEIEVELLY LLIESLKKLN IDESSMPILL INHISLMELI ISKFSKSSKE
     KVTDILSNFD LIEIEKLELD FDERNTLKLL QELRGSPRNV IKTLESLYGN NKILDSLTKI
     FNIIEPISNK YNIQLQLDPT FKPHYELYTG IVFELVCNTR ETPVVIARGG RYDELVKMFN
     ENPEDEIAAG FSYSIDKIRE LNTRLETFDT NPERILVAYG PNKTIKDAIE CQAKLHEKGY
     VAIIELNSCI NEDHAMKLVN QRKCTKLKWI NS