RAPZ_YERPY
ID RAPZ_YERPY Reviewed; 284 AA.
AC B1JKK0;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=YPK_0502;
OS Yersinia pseudotuberculosis serotype O:3 (strain YPIII).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YPIII;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis YPIII.";
RL Submitted (FEB-2008) 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; CP000950; ACA66805.1; -; Genomic_DNA.
DR RefSeq; WP_002210113.1; NZ_CP009792.1.
DR AlphaFoldDB; B1JKK0; -.
DR SMR; B1JKK0; -.
DR PRIDE; B1JKK0; -.
DR EnsemblBacteria; ACA66805; ACA66805; YPK_0502.
DR GeneID; 66844052; -.
DR KEGG; ypy:YPK_0502; -.
DR PATRIC; fig|502800.11.peg.1112; -.
DR OMA; TVMSFGF; -.
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; RNA-binding.
FT CHAIN 1..284
FT /note="RNase adapter protein RapZ"
FT /id="PRO_1000130800"
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; 32533 MW; 5A241B82E7EC30AE CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPQL ASTLADRNIS AAVSIDVRNM
PESPEVFEHA MTQLPDSFSP QLLFLDADRN TLIRRYSDTR RLHPLSAKNL SLESAIDEES
DLLEPLRSRA DLIIDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
FDVRFLPNPH WDPKLRPMTG LDKPVISFLD RHTEVHNFIY QTRSYLEQWL PMLETNNRSY
LTVAIGCTGG KHRSVYVAEQ LADYFRARGK NVQSRHRTLE KRKQ