ID   HISZ_PROMP              Reviewed;         383 AA.
AC   Q7TU96;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; OrderedLocusNames=PMM0900;
OS   Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 /
OS   MED4).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCMP1986 / NIES-2087 / MED4;
RX   PubMed=12917642; DOI=10.1038/nature01947;
RA   Rocap G., Larimer F.W., Lamerdin J.E., Malfatti S., Chain P., Ahlgren N.A.,
RA   Arellano A., Coleman M., Hauser L., Hess W.R., Johnson Z.I., Land M.L.,
RA   Lindell D., Post A.F., Regala W., Shah M., Shaw S.L., Steglich C.,
RA   Sullivan M.B., Ting C.S., Tolonen A., Webb E.A., Zinser E.R.,
RA   Chisholm S.W.;
RT   "Genome divergence in two Prochlorococcus ecotypes reflects oceanic niche
RT   differentiation.";
RL   Nature 424:1042-1047(2003).
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; BX548174; CAE19359.1; -; Genomic_DNA.
DR   RefSeq; WP_011132533.1; NC_005072.1.
DR   AlphaFoldDB; Q7TU96; -.
DR   SMR; Q7TU96; -.
DR   STRING; 59919.PMM0900; -.
DR   EnsemblBacteria; CAE19359; CAE19359; PMM0900.
DR   KEGG; pmm:PMM0900; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_2_3; -.
DR   OMA; KLWGYEE; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001026; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.30.930.10; -; 1.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR041715; HisRS-like_core.
DR   InterPro; IPR004516; HisRS/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_0000171051"
SQ   SEQUENCE   383 AA;  44195 MW;  3061FEB35C13A42B CRC64;
     MSDIKEFNLI DVRNNSSIVN DLNNVYKLWG YEEISPSFIN NLETIKGREV IDGDELIGIV
     SNSSLCLRPE MTTSIVKLTS TRLLNKKRPI RLFNSGIVFN KKQSYKNTYK FQENLQSGIE
     LISYDTQYPE IEVINILFDA IDNINLIDSC NLTLLVSTTK IMDLILFNYK NNNYEEIKKC
     MVNLDHESLD KLNIDNNDKA ILKELLFTRG EPAIILKKLK NIYGNNNVIE ELDCLFNTLS
     KISKKYNIKI QLDPTYQPHL NLYAGIVFQL ICDNKNVKTI IAKGGRYDEL VRYFNPNEKI
     INGIGFTISI DNLRELIVEK SQTKKKVLLL FKNSYLLDKG INEQKALQKK GIITILYLNP
     CNDNSKANIL MKEHNCTEIQ WIK