ID   RAPZ_SODGM              Reviewed;         284 AA.
AC   Q2NWK4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=SG0196;
OS   Sodalis glossinidius (strain morsitans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Bruguierivoracaceae; Sodalis.
OX   NCBI_TaxID=343509;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=morsitans;
RX   PubMed=16365377; DOI=10.1101/gr.4106106;
RA   Toh H., Weiss B.L., Perkin S.A.H., Yamashita A., Oshima K., Hattori M.,
RA   Aksoy S.;
RT   "Massive genome erosion and functional adaptations provide insights into
RT   the symbiotic lifestyle of Sodalis glossinidius in the tsetse host.";
RL   Genome Res. 16:149-156(2006).
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; AP008232; BAE73471.1; -; Genomic_DNA.
DR   RefSeq; WP_011410060.1; NZ_LN854557.1.
DR   AlphaFoldDB; Q2NWK4; -.
DR   SMR; Q2NWK4; -.
DR   STRING; 343509.SG0196; -.
DR   EnsemblBacteria; BAE73471; BAE73471; SG0196.
DR   KEGG; sgl:SG0196; -.
DR   eggNOG; COG1660; Bacteria.
DR   HOGENOM; CLU_059558_1_1_6; -.
DR   OMA; TVMSFGF; -.
DR   OrthoDB; 1603998at2; -.
DR   BioCyc; SGLO343509:SGP1_RS01895-MON; -.
DR   Proteomes; UP000001932; 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; RNA-binding.
FT   CHAIN           1..284
FT                   /note="RNase adapter protein RapZ"
FT                   /id="PRO_0000259001"
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;  32214 MW;  6E44B5651EFEEB04 CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPQL ASALAASNIS AAVSIDVRNM
     PESPEIFEQA MDNLPQAFAP QLLFLDADRN TLIRRYSDTR RLHPLSALNL SLESAIDEED
     SLLEPLRSRA DLVIDTSEMS VHELAEMLRT RMLGKREREL TMVFESFGYK HGIPIDADYV
     FDVRFLPNPH WDPKLRPMTG LDRPVAAFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
     LTVAVGCTGG KHRSVYIAEQ LADYFRSRGK NAQSRHRTLE KSKS