ID   HISZ_PROM1              Reviewed;         391 AA.
AC   A2C228;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=NATL1_09801;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
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; CP000553; ABM75538.1; -; Genomic_DNA.
DR   RefSeq; WP_011823664.1; NC_008819.1.
DR   AlphaFoldDB; A2C228; -.
DR   SMR; A2C228; -.
DR   STRING; 167555.NATL1_09801; -.
DR   EnsemblBacteria; ABM75538; ABM75538; NATL1_09801.
DR   KEGG; pme:NATL1_09801; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_3; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002592; 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.
DR   TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis.
FT   CHAIN           1..391
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000016273"
SQ   SEQUENCE   391 AA;  43906 MW;  36E271953559E243 CRC64;
     MTLQPASGAR DLNPQQVRKN HLIASKLSSL YQLWGYERIS PPHIERLDTL TAAGGISNNE
     ILKIVSDEPL GLRPEITASI VRAASTRFNE YERPLRFWSA GTSFKCNQSI DGGIDIEESF
     QSGVELIGTK AINAEIELLS LLIESLEVIE IDQKYKMTLL IGNTYLLELI LSSFDSTKID
     QIKKILCDLD YIALTTLDVK EEQRMFIKTI MNMRGKPEEV LTNLQNIYGS NSYIDKLKEL
     FTIIEPLAKE KGIEVQLDPT LGTKYKLYSG LTFSLVSSST SAPVTIAKGG RYDDLVKKFS
     SSAQNCYGIG FSISVDKVRE LVSTSKEKLV NNVKVLIAYK QSANLYKALK QQKELHRKGI
     ISVISHEPLK TNDETNQLLK SNRCNKIEWI D