ID   HISZ_RUMCH              Reviewed;         419 AA.
AC   B8I5U8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Ccel_0380;
OS   Ruminiclostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 /
OS   H10) (Clostridium cellulolyticum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Ruminiclostridium.
OX   NCBI_TaxID=394503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35319 / DSM 5812 / JCM 6584 / H10;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Chertkov O., Saunders E., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Zhou J., Richardson P.;
RT   "Complete sequence of Clostridium cellulolyticum H10.";
RL   Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001348; ACL74765.1; -; Genomic_DNA.
DR   RefSeq; WP_012634828.1; NC_011898.1.
DR   AlphaFoldDB; B8I5U8; -.
DR   SMR; B8I5U8; -.
DR   STRING; 394503.Ccel_0380; -.
DR   EnsemblBacteria; ACL74765; ACL74765; Ccel_0380.
DR   KEGG; cce:Ccel_0380; -.
DR   eggNOG; COG0124; Bacteria.
DR   HOGENOM; CLU_025113_0_2_9; -.
DR   OMA; ELVMPPM; -.
DR   OrthoDB; 1236894at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000001349; 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..419
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000122666"
SQ   SEQUENCE   419 AA;  47475 MW;  9DEBD5FA104E5502 CRC64;
     MSRWKIYTPD GVQDILFDEC YKKREIEKRI RNTFRSYGYY EIETPTIEFF DVFSSEIEHF
     PQESMVKFFD QKGRILVLRP DITVPVARIT ATKNRDVQVP IKYSYIGNVF RFNEVGGGRQ
     NEFTQAGVEM LGDSSSESDA EIIAMAINTL KSVGLKEFKI EIGQVEFFKG LAEEAGFSNE
     DIDAISKQID KKDLVGVEEI LNRYDISTEL REIVLKLTGL FGSVDVIKEF KKASINGRSL
     KAIENVEEVV SILCDYGLSE YVSIDLGMLK SLNYDTGITF RGFTNGVGFP ILSGARYDNL
     TSSFGKECPA TGFSLRINML MTAMEKAGHT FERPSVDSLV CYEKTNRKRA IEIAEALRKQ
     DMKIETFVLT KGIDQAKKYA ASKKIGGIIY IRDNDKITVY DIKNNITEET SFDTLLNNQ