ID   RAPZ_HAMD5              Reviewed;         284 AA.
AC   C4K7I7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=HDEF_1942;
OS   Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts; Candidatus Hamiltonella.
OX   NCBI_TaxID=572265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AT;
RX   PubMed=19451630; DOI=10.1073/pnas.0900194106;
RA   Degnan P.H., Yu Y., Sisneros N., Wing R.A., Moran N.A.;
RT   "Hamiltonella defensa, genome evolution of protective bacterial
RT   endosymbiont from pathogenic ancestors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:9063-9068(2009).
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; CP001277; ACQ68530.1; -; Genomic_DNA.
DR   RefSeq; WP_015874289.1; NC_012751.1.
DR   AlphaFoldDB; C4K7I7; -.
DR   SMR; C4K7I7; -.
DR   STRING; 572265.HDEF_1942; -.
DR   EnsemblBacteria; ACQ68530; ACQ68530; HDEF_1942.
DR   GeneID; 66261513; -.
DR   KEGG; hde:HDEF_1942; -.
DR   eggNOG; COG1660; Bacteria.
DR   HOGENOM; CLU_059558_1_1_6; -.
DR   OMA; TVMSFGF; -.
DR   Proteomes; UP000002334; 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   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..284
FT                   /note="RNase adapter protein RapZ"
FT                   /id="PRO_1000212363"
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;  32744 MW;  A108814C1285A739 CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPIILLPNL ASSLMPRNTP AAISIDVRNM
     PGSSEIFEKV LTKLNKKFST RLIFLDANHN TLIQRYSETR RLHPLSGNHL SLEKAIDEEN
     ILLEPLRSRA DLIINTSEMS VHQLSEMLRV RSLGTKERKL SMVFESFGFK YGLPIYADYV
     FDVRFLPNPH WDPKLRSMTG LDKPVVDFLK RHSEVHHFIY QTLHYLNQWL PMLENNDRSY
     LTIAIGCTGG KHRSVYIAEQ LADYFRSRGK NVQLRHRTLE KRKE