HISZ_STAEQ
ID HISZ_STAEQ Reviewed; 270 AA.
AC Q5HKN6;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
DE RecName: Full=ATP phosphoribosyltransferase regulatory subunit;
GN Name=hisZ; OrderedLocusNames=SERP2307;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW53204.1; -; Genomic_DNA.
DR RefSeq; WP_002470288.1; NC_002976.3.
DR AlphaFoldDB; Q5HKN6; -.
DR SMR; Q5HKN6; -.
DR STRING; 176279.SERP2307; -.
DR EnsemblBacteria; AAW53204; AAW53204; SERP2307.
DR KEGG; ser:SERP2307; -.
DR eggNOG; COG3705; Bacteria.
DR HOGENOM; CLU_089652_0_0_9; -.
DR OMA; RYYSNYP; -.
DR OrthoDB; 1236894at2; -.
DR UniPathway; UPA00031; UER00006.
DR Proteomes; UP000000531; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.30.930.10; -; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR041715; HisRS-like_core.
DR Pfam; PF13393; tRNA-synt_His; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cytoplasm; Histidine biosynthesis;
KW Reference proteome.
FT CHAIN 1..270
FT /note="ATP phosphoribosyltransferase regulatory subunit"
FT /id="PRO_0000171066"
SQ SEQUENCE 270 AA; 32150 MW; 15B6FAED5195DE96 CRC64;
MNNTIISMKE KELRFLKFFH QQKYNVVDFN LIEELDWQRL THEDLQQMDE RSFWQQNKSI
YALRNDFTDQ LFRYYSNYPT HFKKVAYAGD IIRDNRVIKQ VGIENYEPQF DNITQNFLDF
QYFIQNVLHD DIQFIILGHY QLIDALLEKN HQTREVMEMI EERNLSGLIQ TLTFNHPIIQ
ILKENTLNQL KILSHYLPER HPAMVAIQSW SQWFTDHGIT EIHLDVTAQA PRSYYKGIFI
KCHLKNTAHS VLTGGYYHGS LEGFGLGLTL