RAPZ_SALPA
ID RAPZ_SALPA Reviewed; 284 AA.
AC Q5PLD3;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=SPA3190;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000026; AAV79015.1; -; Genomic_DNA.
DR RefSeq; WP_000243749.1; NC_006511.1.
DR AlphaFoldDB; Q5PLD3; -.
DR SMR; Q5PLD3; -.
DR EnsemblBacteria; AAV79015; AAV79015; SPA3190.
DR KEGG; spt:SPA3190; -.
DR HOGENOM; CLU_059558_1_1_6; -.
DR OMA; TVMSFGF; -.
DR Proteomes; UP000008185; 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..284
FT /note="RNase adapter protein RapZ"
FT /id="PRO_0000107750"
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; 32464 MW; EFBF65E875D74012 CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPDL ARTLADRQIS AAVSIDVRNM
PESPEIFEQA MNNLPGAFSP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLESAIDKES
DLLEPLRSRA DLIVDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
FDVRFLPNPH WDPKLRPMTG LDKPVAAFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
LTVAIGCTGG KHRSVYIAEQ LADYFRSRGK NVQSRHRTLE KRKT
