ID   HISZ_BRUA2              Reviewed;         378 AA.
AC   Q2YIH8;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-JUN-2006, sequence version 2.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=BAB2_0182;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAJ12348.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AM040265; CAJ12348.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q2YIH8; -.
DR   SMR; Q2YIH8; -.
DR   STRING; 359391.BAB2_0182; -.
DR   EnsemblBacteria; CAJ12348; CAJ12348; BAB2_0182.
DR   KEGG; bmf:BAB2_0182; -.
DR   HOGENOM; CLU_025113_6_0_5; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002719; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
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.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..378
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_0000242825"
SQ   SEQUENCE   378 AA;  40921 MW;  E827A4A65543E4E2 CRC64;
     MTMVGSRTSP IFNALRVELN AREAELVEIP LIQPADPFLD MAGEDLRRRI FLTENENGDS
     LCLRPEFTIP VCRNHIALNA ATPKRYAYLG EVFRQRRDGA AEFLQAGIED LGAADEAASD
     ARSLADALSC VKAIAPDAPL EIVLGDQSVF AGMLKALGLP QGWRKKLLRS FGDAHSMDLA
     LAELTGTQRR DPLPESLAVL VAEGDEIGLA RMLEAEMLEA GISPGAGRTP VEIARRLIEK
     EDLAATHFPA AALDLLRQFL AIRVSLDMAA VTLRAFAADN ALDLGAVLQK FEARADAIAQ
     AGIEMKDIIY DASFGRPLDY YTGLVYEIRD ASNRQDGVLA GGGRYDRLLT MLGACEAIPG
     VGFSIWLDRL QALAGEKQ