ID   HISZ_BRUA4              Reviewed;         376 AA.
AC   A6X3C2;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=ATP phosphoribosyltransferase regulatory subunit {ECO:0000255|HAMAP-Rule:MF_00125};
GN   Name=hisZ {ECO:0000255|HAMAP-Rule:MF_00125}; OrderedLocusNames=Oant_3018;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(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; CP000759; ABS15726.1; -; Genomic_DNA.
DR   RefSeq; WP_011982739.1; NC_009668.1.
DR   AlphaFoldDB; A6X3C2; -.
DR   SMR; A6X3C2; -.
DR   STRING; 439375.Oant_3018; -.
DR   PRIDE; A6X3C2; -.
DR   EnsemblBacteria; ABS15726; ABS15726; Oant_3018.
DR   KEGG; oan:Oant_3018; -.
DR   PATRIC; fig|439375.7.peg.3170; -.
DR   eggNOG; COG3705; Bacteria.
DR   HOGENOM; CLU_025113_6_0_5; -.
DR   OMA; YYTGFEF; -.
DR   OrthoDB; 277998at2; -.
DR   UniPathway; UPA00031; UER00006.
DR   Proteomes; UP000002301; Chromosome 2.
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..376
FT                   /note="ATP phosphoribosyltransferase regulatory subunit"
FT                   /id="PRO_1000095464"
SQ   SEQUENCE   376 AA;  40568 MW;  7B45221F29085CF1 CRC64;
     MAGSSSSGVF NSLRATLDMR EAELVEIPLI QPADPFLDMA GEDLRRRIFL TENENGDSLC
     LRPEFTIPVC RNHIALNAAT PKRYAYLGEV FRQHRDGAAE FLQAGIEDLG ASDEAASDAR
     SIADALSCVR AAAPEAELEI VLGDQSVFAG MLKALGLPQG WRKKLLRSFG DANSMEQVLA
     ELTGAQRRDP LPETLAGLVA EGDESGLARM LEAEMLEAGI SPSAGRSPAE IARRLIEKED
     LAATRFPASA LDLLKQFLET RVTLDSAAVT LRAFASEHAL DLAAVLQKFE ARSEAIANAG
     IATKDIIYDA SFGRPLDYYT GLVYEIRAPG VEKEGVLAGG GRYDRLLTML GASENIPGVG
     FSIWLDRLQM LVGEKK