ID   HISZ_LEPIN              Reviewed;         344 AA.
AC   Q8F737;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; Synonyms=hisS2; OrderedLocusNames=LA_1111;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(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; AE010300; AAN48310.1; -; Genomic_DNA.
DR   RefSeq; NP_711292.1; NC_004342.2.
DR   RefSeq; WP_001075198.1; NC_004342.2.
DR   AlphaFoldDB; Q8F737; -.
DR   SMR; Q8F737; -.
DR   STRING; 189518.LA_1111; -.
DR   EnsemblBacteria; AAN48310; AAN48310; LA_1111.
DR   GeneID; 61142442; -.
DR   KEGG; lil:LA_1111; -.
DR   PATRIC; fig|189518.3.peg.1102; -.
DR   HOGENOM; CLU_025113_0_2_12; -.
DR   InParanoid; Q8F737; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
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   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..344
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171041"
SQ   SEQUENCE   344 AA;  39114 MW;  4891578AD80DB983 CRC64;
     MNQNLPEPNQ KKWIPDGFHF LGPEDSKYRR TLLETISGVL KKKGYSEVFL PAFDYSSTFI
     QTVSAPDSSS LFRIRDLSGN EISPSIDLTV QAVKGMAGFS HQRENQNIFY IGRVFRESTK
     GSVARKEILQ IGAESIGVSG KENTFKILEE LDEIISLLPL ENKLTLVLGN VNLFQSIVQE
     FELKQNEIEI LSKLLYQKNV NEIQKIFGEK KNHTDLIRLL SSLVLNFDLN SLKNSLNINS
     LSKNLQKSLS SILEETYWIF NSWESKKRRI DLCIDFSLLR DLNYYTGFVF QGYLQDSPDP
     VLTGGTYDHL YEMFSGVQKN ASGYALMVNT LESSLKTPLF NLSS