HISZ_LISMO
ID HISZ_LISMO Reviewed; 393 AA.
AC Q8Y9F9;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN Name=hisZ; OrderedLocusNames=lmo0569;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(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; AL591975; CAC98648.1; -; Genomic_DNA.
DR PIR; AB1146; AB1146.
DR RefSeq; NP_464097.1; NC_003210.1.
DR RefSeq; WP_003721363.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y9F9; -.
DR SMR; Q8Y9F9; -.
DR STRING; 169963.lmo0569; -.
DR PaxDb; Q8Y9F9; -.
DR EnsemblBacteria; CAC98648; CAC98648; CAC98648.
DR GeneID; 984506; -.
DR KEGG; lmo:lmo0569; -.
DR PATRIC; fig|169963.11.peg.588; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_025113_0_0_9; -.
DR OMA; ELVMPPM; -.
DR PhylomeDB; Q8Y9F9; -.
DR BioCyc; LMON169963:LMO0569-MON; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000817; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00773; HisRS-like_core; 1.
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.
DR TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..393
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171044"
SQ SEQUENCE 393 AA; 44034 MW; 85F09F30429CCFC4 CRC64;
MNLNKNLPTG TRDKLFREAR AAYKIEQQVN HYFEKRGFKR IETPVIEFED VFSSEHQADA
KLYRFFDEKG RLTVLRPDMT LPIGRVVSTT GVMLPLKLSY SGKIFRANED FGGEQNEQTQ
AGIEIIGYPS IKAEIECILI GIGVLNALEI PNFQIELGHA AIYRRVTNLL NLSETAEIDF
RLLIQNKSLT GIKRFVADNP STLDDFILAL PRLFGPATAI LKQAKNLTTD KGILTALREM
ETIVEAVSYT ADISVDLGLV QDFHYYTGII FRGYADLAAD NFLSGGRYDH LLEQFTSASS
PAVGLALNLD SLTTLQNRAG VIKKQVSTSL LIHYDLDAIQ QAEKLMQETP NSELSFFETP
TNAISFAKKW HIPAVIHVSR QGIQTIFQRE ADL