ID   HISZ_LISMH              Reviewed;         392 AA.
AC   B8DA56;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=LMHCC_2062;
OS   Listeria monocytogenes serotype 4a (strain HCC23).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=552536;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HCC23;
RX   PubMed=21602330; DOI=10.1128/jb.05236-11;
RA   Steele C.L., Donaldson J.R., Paul D., Banes M.M., Arick T., Bridges S.M.,
RA   Lawrence M.L.;
RT   "Genome sequence of lineage III Listeria monocytogenes strain HCC23.";
RL   J. Bacteriol. 193:3679-3680(2011).
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; CP001175; ACK40401.1; -; Genomic_DNA.
DR   RefSeq; WP_003729310.1; NC_011660.1.
DR   AlphaFoldDB; B8DA56; -.
DR   SMR; B8DA56; -.
DR   KEGG; lmh:LMHCC_2062; -.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   UniPathway; UPA00031; UER00006.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00773; HisRS-like_core; 1.
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..392
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000122673"
SQ   SEQUENCE   392 AA;  43884 MW;  0E75A1D4183B0E79 CRC64;
     MNLNKNLPTG TRDKLFREAQ AAYKIEQQVN HYFEKRGFKR IETPVIEFED VFSSEHQADA
     KLYRFFDEKG RLTVLRPDMT LPIGRVVSTT GVTLPLKLSY SGKIFRANED FGGEQNEQTQ
     AGIEIIGYPS IKAEIECILS GIGVLNALEI PNFQIELGHA AIYRRVIQLL NLSETAEIDF
     RQLIQNKSLT GIKRFVANNP STLDDFILAI PRLFGPATAI LSQAKNLTTD KGILTALHEM
     ETIVEAVSYT ADISVDLGLV QDFHYYTGII FRGYADLAAD NFLSGGRYDH LLEQFTSSSS
     PAVGLALNLD SLTTLQNRAG IIKKQTPTTL LIHYDLEALQ QAEKFMQETP NSELSFFETA
     SNAISFAKKW HIPEVVHVSS QGIQTIFQRE VD