ID   RAPZ_KLEOX              Reviewed;         284 AA.
AC   P17163;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 3.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636};
OS   Klebsiella oxytoca.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=M5a1;
RA   Merrick M.J., Taylor M.;
RT   "Sequence and characterisation of distal genes in the Klebsiella pneumoniae
RT   rpoN operon.";
RL   Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-193.
RC   STRAIN=M5a1;
RX   PubMed=2695747; DOI=10.1111/j.1365-2958.1989.tb00162.x;
RA   Merrick M.J., Coppard J.R.;
RT   "Mutations in genes downstream of the rpoN gene (encoding sigma 54) of
RT   Klebsiella pneumoniae affect expression from sigma 54-dependent
RT   promoters.";
RL   Mol. Microbiol. 3:1765-1775(1989).
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; Z50803; CAA90684.1; -; Genomic_DNA.
DR   EMBL; X16335; CAA34393.1; -; Genomic_DNA.
DR   PIR; S60666; S60666.
DR   RefSeq; WP_004106169.1; NZ_WVTN01000004.1.
DR   AlphaFoldDB; P17163; -.
DR   SMR; P17163; -.
DR   STRING; 571.MC52_05310; -.
DR   GeneID; 64335455; -.
DR   GeneID; 66587664; -.
DR   eggNOG; COG1660; Bacteria.
DR   OrthoDB; 1603998at2; -.
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; RNA-binding.
FT   CHAIN           1..284
FT                   /note="RNase adapter protein RapZ"
FT                   /id="PRO_0000107718"
FT   REGION          266..284
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   284 AA;  32523 MW;  F81343CA5FEFC67B CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPEL ARSLADRNIS AAVSIDVRNM
     PESPEIFEQA MKNLPAEFSP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLESAIDEES
     DLLEPLRSRA DLIVDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
     FDVRFLPNPH WDPKLRPMTG LDKPVAAFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
     LTVAIGCTGG KHRSVYIAEQ LADYFRSRGK NVQSRHRTLE KRKS