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Database: UniProt
Entry: D3VDI5_XENNA
LinkDB: D3VDI5_XENNA
Original site: D3VDI5_XENNA 
ID   D3VDI5_XENNA            Unreviewed;       283 AA.
AC   D3VDI5;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN   OrderedLocusNames=XNC1_4200 {ECO:0000313|EMBL:CBJ92225.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG
OS   1036 / NCIMB 9965 / AN6).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ92225.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|EMBL:CBJ92225.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 /
RC   AN6 {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA   Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA   Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA   Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA   Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA   Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA   Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA   van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA   Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA   Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT   convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:E27909-E27909(2011).
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; FN667742; CBJ92225.1; -; Genomic_DNA.
DR   RefSeq; WP_010847736.1; NC_014228.1.
DR   AlphaFoldDB; D3VDI5; -.
DR   STRING; 406817.XNC1_4200; -.
DR   KEGG; xne:XNC1_4200; -.
DR   eggNOG; COG1660; Bacteria.
DR   HOGENOM; CLU_059558_1_1_6; -.
DR   Proteomes; UP000008075; 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; P-loop containing nucleotide triphosphate hydrolases; 1.
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:UP000008075};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00636}.
FT   REGION          266..283
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   283 AA;  32422 MW;  75E5487B9077B936 CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPEL ASTLAERDIS AAVSIDVRNM
     PESPEIFEEA LTQLPDNFSP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLESAIDQES
     DLLEPLRSRA DLIIDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
     FDVRFLPNPH WDPKLRPMTG LDRPVAAFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
     LTVAIGCTGG KHRSVYVAEQ LADYFRSRGK NVQSRHRTLE KRK
//
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