ID   HISZ_CLOAB              Reviewed;         407 AA.
AC   Q97KI4;
DT   15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN   Name=hisZ; OrderedLocusNames=CA_C0935;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
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; AE001437; AAK78911.1; -; Genomic_DNA.
DR   PIR; D97015; D97015.
DR   RefSeq; NP_347571.1; NC_003030.1.
DR   RefSeq; WP_010964253.1; NC_003030.1.
DR   AlphaFoldDB; Q97KI4; -.
DR   SMR; Q97KI4; -.
DR   STRING; 272562.CA_C0935; -.
DR   PRIDE; Q97KI4; -.
DR   EnsemblBacteria; AAK78911; AAK78911; CA_C0935.
DR   GeneID; 44997445; -.
DR   KEGG; cac:CA_C0935; -.
DR   PATRIC; fig|272562.8.peg.1145; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_0_0_9; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000000814; Chromosome.
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; IPR006195; aa-tRNA-synth_II.
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.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..407
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000171033"
SQ   SEQUENCE   407 AA;  46248 MW;  10E3380EC654D6FC CRC64;
     MINLKKYIPE GSRDILFEEC TIKNNIENIL RNSYINVGYE EVRSPTLEFY DVYNLENQPI
     SQEKMYKLFD NTGRILVLRP DMTTPIARIC ATKLKNRVYP LKLSYTGNIY RMNKALNGKI
     SEITQSGIEI LGFSSLKADA EVIITAIKAI LKTGLKNFKI EIGQVEFFKS IISDTALKEQ
     DTEKLRNFIE NKNFSKVEEF ILRNSDLIGE TSSKVLMNLP NLFGGKEVIE KAEQLTSNKQ
     AIEALKKVRD LYDIVKRAGF GEYILIDLGM VQHINYYTGL IFRGYAHGIG DDLLSGGRYD
     KLLGQFGYDI PATGLAINVD NLVAALDDCV RENLYSRDRY VVFASSCNIE KAYEAVSKLN
     SEGKRAEVSL FDNIEETKKY CIENKISKIF NADTGKTIVE ENYYGQK