ID   RAPZ_PECCP              Reviewed;         285 AA.
AC   C6DIN0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   03-AUG-2022, entry version 56.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=PC1_0271;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-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; CP001657; ACT11330.1; -; Genomic_DNA.
DR   RefSeq; WP_010296630.1; NC_012917.1.
DR   AlphaFoldDB; C6DIN0; -.
DR   SMR; C6DIN0; -.
DR   STRING; 561230.PC1_0271; -.
DR   EnsemblBacteria; ACT11330; ACT11330; PC1_0271.
DR   GeneID; 51387735; -.
DR   GeneID; 61410577; -.
DR   KEGG; pct:PC1_0271; -.
DR   eggNOG; COG1660; Bacteria.
DR   HOGENOM; CLU_059558_1_1_6; -.
DR   OMA; TVMSFGF; -.
DR   OrthoDB; 1603998at2; -.
DR   Proteomes; UP000002736; 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..285
FT                   /note="RNase adapter protein RapZ"
FT                   /id="PRO_1000212364"
FT   REGION          266..285
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   285 AA;  32572 MW;  FFCF4F477E7AC19A CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPEL ANTLAARNIS AAVSIDVRNM
     PESPEIFEHA MEQLPPSFSP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLESAIDEES
     DLLEPLRSRA DLIIDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
     FDVRFLPNPH WDPKLRPMTG LDKPVASFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
     LTVAIGCTGG KHRSVYVAEQ LADYFRSRGK NVQSRHRTLE KRKPS