(data stored in ACNUC7421 zone)

SWISSPROT: RAPZ_EDWI9

ID   RAPZ_EDWI9              Reviewed;         283 AA.
AC   C5B725;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 52.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN   OrderedLocusNames=NT01EI_0570;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Modulates the synthesis of GlmS, by affecting the
CC       processing and stability of the regulatory small RNA GlmZ. When
CC       glucosamine-6-phosphate (GlcN6P) concentrations are high in the
CC       cell, RapZ binds GlmZ and targets it to cleavage by RNase E.
CC       Consequently, GlmZ is inactivated and unable to activate GlmS
CC       synthesis. Under low GlcN6P concentrations, RapZ is sequestered
CC       and inactivated by an other regulatory small RNA, GlmY, preventing
CC       GlmZ degradation and leading to synthesis of GlmS.
CC       {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}.
DR   EMBL; CP001600; ACR67799.1; -; Genomic_DNA.
DR   RefSeq; WP_015869998.1; NC_012779.2.
DR   SMR; C5B725; -.
DR   EnsemblBacteria; ACR67799; ACR67799; NT01EI_0570.
DR   GeneID; 7960338; -.
DR   KEGG; eic:NT01EI_0570; -.
DR   PATRIC; fig|634503.3.peg.515; -.
DR   eggNOG; ENOG4105C21; Bacteria.
DR   eggNOG; COG1660; LUCA.
DR   HOGENOM; HOG000244885; -.
DR   KO; K06958; -.
DR   OMA; TVMSFGF; -.
DR   OrthoDB; 1603998at2; -.
DR   BioCyc; EICT634503:G1GVC-531-MONOMER; -.
DR   Proteomes; UP000001485; 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;
DR   PRODOM; C5B725.
DR   SWISS-2DPAGE; C5B725.
KW   ATP-binding; Complete proteome; GTP-binding; Nucleotide-binding;
KW   Reference proteome; RNA-binding.
FT   CHAIN         1    283       RNase adapter protein RapZ.
FT                                /FTId=PRO_1000212360.
FT   NP_BIND       8     15       ATP. {ECO:0000255|HAMAP-Rule:MF_00636}.
FT   NP_BIND      56     59       GTP. {ECO:0000255|HAMAP-Rule:MF_00636}.
FT   REGION      266    283       RNA-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00636}.
SQ   SEQUENCE   283 AA;  32425 MW;  7DCFFE0CFBDD1977 CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVELLPEL ARTLATRDTS AAVSIDVRNM
     PESPEVLETA MDHLPESFTP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLENAIDQEN
     ELLEPLRSRA DLIIDTSEMS VHELAEMLRA RLLGKREREL TMVFESFGFK HGIPIDADYV
     FDVRFLPNPH WDPKLRPMTG LDKPVAAFLD RHTEVHNFIY QTRSYLEQWL PALENNNRSY
     LTVAIGCTGG KHRSVYVAEQ LADYFRSRGK NVQSRHRTLE KRK
//

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