ID A0A411WNK5_9GAMM Unreviewed; 290 AA.
AC A0A411WNK5;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000256|HAMAP-Rule:MF_00636,
GN ECO:0000313|EMBL:QBH97814.1};
GN ORFNames=EKN56_16220 {ECO:0000313|EMBL:QBH97814.1};
OS Limnobaculum zhutongyuii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Budviciaceae; Limnobaculum.
OX NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH97814.1, ECO:0000313|Proteomes:UP000293154};
RN [1] {ECO:0000313|EMBL:QBH97814.1, ECO:0000313|Proteomes:UP000293154}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF-458 {ECO:0000313|EMBL:QBH97814.1,
RC ECO:0000313|Proteomes:UP000293154};
RA Ge Y.;
RT "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL Submitted (MAR-2019) 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: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; CP034752; QBH97814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A411WNK5; -.
DR KEGG; prag:EKN56_16220; -.
DR OrthoDB; 9784461at2; -.
DR Proteomes; UP000293154; 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: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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_00636}.
FT REGION 266..290
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 290 AA; 33155 MW; DE2B459AE53999D7 CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPQL AETLAERQTS AAVSIDVRNL
PETPEILEEV LNNLPGDFSP QLLFLDADRN TLIRRYSDTR RLHPLSNKNL SLESAIDEED
TLLEPLRSRA DLIIDTAEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
FDVRFLPNPH WDPKLRPMTG LDKPVASFLD RHTEVHNFIY QTRSYLEQWL PMLETNNRSY
LTVAIGCTGG KHRSVYVAEQ LADYFRSRGK NVQSRHRTLE KRKNDGKNSN
//
