ID   RAPZ_EDWI9              Reviewed;         283 AA.
AC   C5B725;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=NT01EI_0570;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Modulates the synthesis of GlmS, by affecting the processing
CC       and stability of the regulatory small RNA GlmZ. When glucosamine-6-
CC       phosphate (GlcN6P) concentrations are high in the cell, RapZ binds GlmZ
CC       and targets it to cleavage by RNase E. Consequently, GlmZ is
CC       inactivated and unable to activate GlmS synthesis. Under low GlcN6P
CC       concentrations, RapZ is sequestered and inactivated by an other
CC       regulatory small RNA, GlmY, preventing GlmZ degradation and leading to
CC       synthesis of GlmS. {ECO:0000255|HAMAP-Rule:MF_00636}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_00636}.
CC   -!- SIMILARITY: Belongs to the RapZ-like family. RapZ subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00636}.
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DR   EMBL; CP001600; ACR67799.1; -; Genomic_DNA.
DR   RefSeq; WP_015869998.1; NC_012779.2.
DR   AlphaFoldDB; C5B725; -.
DR   SMR; C5B725; -.
DR   STRING; 67780.B6E78_13555; -.
DR   EnsemblBacteria; ACR67799; ACR67799; NT01EI_0570.
DR   GeneID; 7960338; -.
DR   KEGG; eic:NT01EI_0570; -.
DR   PATRIC; fig|634503.3.peg.515; -.
DR   HOGENOM; CLU_059558_1_1_6; -.
DR   OMA; TVMSFGF; -.
DR   OrthoDB; 1603998at2; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00636; RapZ_like; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005337; RapZ-like.
DR   PANTHER; PTHR30448; PTHR30448; 1.
DR   Pfam; PF03668; ATP_bind_2; 1.
DR   PIRSF; PIRSF005052; P-loopkin; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; GTP-binding; Nucleotide-binding; Reference proteome;
KW   RNA-binding.
FT   CHAIN           1..283
FT                   /note="RNase adapter protein RapZ"
FT                   /id="PRO_1000212360"
FT   REGION          266..283
FT                   /note="RNA-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT   BINDING         56..59
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
SQ   SEQUENCE   283 AA;  32425 MW;  7DCFFE0CFBDD1977 CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVELLPEL ARTLATRDTS AAVSIDVRNM
     PESPEVLETA MDHLPESFTP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLENAIDQEN
     ELLEPLRSRA DLIIDTSEMS VHELAEMLRA RLLGKREREL TMVFESFGFK HGIPIDADYV
     FDVRFLPNPH WDPKLRPMTG LDKPVAAFLD RHTEVHNFIY QTRSYLEQWL PALENNNRSY
     LTVAIGCTGG KHRSVYVAEQ LADYFRSRGK NVQSRHRTLE KRK