RAPZ_PHOLL
ID RAPZ_PHOLL Reviewed; 283 AA.
AC Q7N053;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=plu4044;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571872; CAE16416.1; -; Genomic_DNA.
DR RefSeq; WP_011148173.1; NC_005126.1.
DR AlphaFoldDB; Q7N053; -.
DR SMR; Q7N053; -.
DR STRING; 243265.plu4044; -.
DR EnsemblBacteria; CAE16416; CAE16416; plu4044.
DR GeneID; 24169616; -.
DR KEGG; plu:plu4044; -.
DR eggNOG; COG1660; Bacteria.
DR HOGENOM; CLU_059558_1_1_6; -.
DR OMA; TVMSFGF; -.
DR OrthoDB; 1603998at2; -.
DR BioCyc; PLUM243265:PLU_RS20030-MON; -.
DR Proteomes; UP000002514; 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;
KW ATP-binding; GTP-binding; Nucleotide-binding; Reference proteome;
KW RNA-binding.
FT CHAIN 1..283
FT /note="RNase adapter protein RapZ"
FT /id="PRO_0000107740"
FT REGION 266..283
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 283 AA; 32364 MW; 8B0140164A9044B4 CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPEL ANTLADRDIS AAVSIDVRNM
PESPEVFEEA LTKLPASFSP QLLFLDAERN TLIRRYSDTR RLHPLSSKNL SLESAIDQES
DLLEPLRSRA DLIIDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
FDVRFLPNPH WDPKLRPMTG LDRPVAAFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
LTVAIGCTGG KHRSVYVAEQ LADYFRSRGK NVQSRHRTLE KRK
