ID E0WRS4_9ENTR Unreviewed; 288 AA.
AC E0WRS4;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN ORFNames=REG_0036 {ECO:0000313|EMBL:EFL92298.1};
OS Candidatus Regiella insecticola LSR1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; aphid secondary symbionts; Regiella.
OX NCBI_TaxID=663321 {ECO:0000313|EMBL:EFL92298.1, ECO:0000313|Proteomes:UP000005726};
RN [1] {ECO:0000313|EMBL:EFL92298.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LSR1 {ECO:0000313|EMBL:EFL92298.1};
RX PubMed=19840097;
RA Degnan P.H., Leonardo T.E., Cass B.N., Hurwitz B., Stern D., Gibbs R.A.,
RA Richards S., Moran N.A.;
RT "Dynamics of genome evolution in facultative symbionts of aphids.";
RL Environ. Microbiol. 0:0-0(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:0000256|HAMAP-Rule:MF_00636}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_00636}.
CC -!- SIMILARITY: Belongs to the RapZ-like family. RapZ subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00636}.
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DR EMBL; GL379589; EFL92298.1; -; Genomic_DNA.
DR RefSeq; WP_006704035.1; NZ_GL379589.1.
DR AlphaFoldDB; E0WRS4; -.
DR STRING; 663321.REG_0036; -.
DR eggNOG; COG1660; Bacteria.
DR HOGENOM; CLU_059558_1_1_6; -.
DR Proteomes; UP000005726; Miscellaneous, Scaffold Scaffold1.
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:SF0; RNASE ADAPTER PROTEIN RAPZ; 1.
DR PANTHER; PTHR30448; UNCHARACTERIZED; 1.
DR Pfam; PF03668; ATP_bind_2; 1.
DR PIRSF; PIRSF005052; P-loopkin; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW Reference proteome {ECO:0000313|Proteomes:UP000005726};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00636}.
FT REGION 265..288
FT /note="RNA-binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00636"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00636"
FT BINDING 56..59
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00636"
SQ SEQUENCE 288 AA; 33084 MW; 4AB9135B956F85E3 CRC64;
MVLIIVSGRS GSGKSVALHA LEDMGFYCVD NLPIVLLPQL VDTLIESNSS AAISIDIRNM
PESPETFAQA IKKLPVKFSP KLLFFDADSN TLIRRYSDTR RLHPLSSKDL SLENAIDKEN
RLLTPLRAVA DFIIDTSQIS VHELDKKLQT YLGKRKRKLS LNFESFGFKY GLPMNADYVF
DVRFLPNPHW DQKLRCMTGL DQPVIDFFEK HIEVRKFINA TGRYLERWLP MLENNNRHYL
TVAVGCTGGQ HRSVYVTEKL VKHFRSKGKI VQLHHRALWK NNNDKKNS
//
