ID D5XD53_THEPJ Unreviewed; 393 AA.
AC D5XD53;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000256|ARBA:ARBA00020397, ECO:0000256|HAMAP-Rule:MF_00125};
GN Name=hisZ {ECO:0000256|HAMAP-Rule:MF_00125};
GN OrderedLocusNames=TherJR_0834 {ECO:0000313|EMBL:ADG81701.1};
OS Thermincola potens (strain JR).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Thermincolaceae;
OC Thermincola.
OX NCBI_TaxID=635013 {ECO:0000313|EMBL:ADG81701.1, ECO:0000313|Proteomes:UP000002377};
RN [1] {ECO:0000313|EMBL:ADG81701.1, ECO:0000313|Proteomes:UP000002377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JR {ECO:0000313|EMBL:ADG81701.1,
RC ECO:0000313|Proteomes:UP000002377};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Hazen T.C., Woyke T.;
RT "Complete sequence of Thermincola sp. JR.";
RL Submitted (MAY-2010) 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:0000256|ARBA:ARBA00025246, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004667, ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SUBUNIT: Heteromultimer composed of HisG and HisZ subunits.
CC {ECO:0000256|ARBA:ARBA00011496, ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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 {ECO:0000256|HAMAP-Rule:MF_00125}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC HisZ subfamily. {ECO:0000256|ARBA:ARBA00005539, ECO:0000256|HAMAP-
CC Rule:MF_00125}.
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DR EMBL; CP002028; ADG81701.1; -; Genomic_DNA.
DR RefSeq; WP_013119722.1; NC_014152.1.
DR AlphaFoldDB; D5XD53; -.
DR STRING; 635013.TherJR_0834; -.
DR KEGG; tjr:TherJR_0834; -.
DR eggNOG; COG0124; Bacteria.
DR HOGENOM; CLU_025113_0_2_9; -.
DR OrthoDB; 9800814at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000002377; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00773; HisRS-like_core; 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 NCBIfam; TIGR00443; hisZ_biosyn_reg; 1.
DR PANTHER; PTHR43707:SF1; HISTIDINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR PANTHER; PTHR43707; HISTIDYL-TRNA SYNTHETASE; 1.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR PIRSF; PIRSF001549; His-tRNA_synth; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Aminoacyl-tRNA synthetase {ECO:0000313|EMBL:ADG81701.1};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00125};
KW Histidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00125};
KW Ligase {ECO:0000313|EMBL:ADG81701.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002377}.
FT DOMAIN 26..326
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 393 AA; 44888 MW; F66A1462E9303A13 CRC64;
MMSRSFKTEI PSGVRDLMPG EAWCKRELER EISDIFRAWG YQEVVTPAFE YFDVLKIGQR
DEQLDLMYKF IDRQGRILAL RPDMTTPIAR LTASRQKRGP FPLRLFYIAN VFSYEEPQAG
RQREYYQAGV ELIGSSNPEA DAEVLALTVE VLKKIGLQNF KLSVGQIDIF NGLMEELEVA
EEVKKEIKTT ISNQNFVGVE EMLHNQKLPE KEIDKVMQII TLRGSRRELE SIRPMLTSAK
ALKALDNLEE VFAVLTDYRL DRYVDLDLGL LRDFDYYTGL VFEGSALGLG FPICGGGRYD
GLLGQFGLPC PATGFALGIE RIMLALERQG HSRDFKNLDY IIEYENHRRL EAFDKAAQLR
AEGHRVVTRD RRSGVQLNSE DSMFSDAKVI TLD
//
