RAPZ_PROMH
ID RAPZ_PROMH Reviewed; 284 AA.
AC Q9ZA87; B4EX44;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000255|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000255|HAMAP-Rule:MF_00636}; OrderedLocusNames=PMI3645;
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10206698; DOI=10.1099/13500872-145-1-185;
RA Zhao H., Li X., Johnson D.E., Mobley H.L.T.;
RT "Identification of protease and rpoN-associated genes of uropathogenic
RT Proteus mirabilis by negative selection in a mouse model of ascending
RT urinary tract infection.";
RL Microbiology 145:185-195(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320;
RX PubMed=18375554; DOI=10.1128/jb.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.T.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
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; AF088980; AAC64575.1; -; Genomic_DNA.
DR EMBL; AM942759; CAR47116.1; -; Genomic_DNA.
DR RefSeq; WP_004245308.1; NC_010554.1.
DR AlphaFoldDB; Q9ZA87; -.
DR SMR; Q9ZA87; -.
DR STRING; 529507.PMI3645; -.
DR EnsemblBacteria; CAR47116; CAR47116; PMI3645.
DR GeneID; 6802621; -.
DR KEGG; pmr:PMI3645; -.
DR eggNOG; COG1660; Bacteria.
DR HOGENOM; CLU_059558_1_1_6; -.
DR OMA; TVMSFGF; -.
DR Proteomes; UP000008319; 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; Reference proteome;
KW RNA-binding.
FT CHAIN 1..284
FT /note="RNase adapter protein RapZ"
FT /id="PRO_0000107743"
FT REGION 267..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 57..60
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00636"
FT CONFLICT 127
FT /note="L -> I (in Ref. 1; AAC64575)"
FT /evidence="ECO:0000305"
FT CONFLICT 131..133
FT /note="ADL -> DVW (in Ref. 1; AAC64575)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 284 AA; 32496 MW; 45C405904E62D70E CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVDLLPEL AKTLAERDAA AAAVSIDVRN
MPESPEIFEK ALESLPAEYS PQLLFLDADR NTLIRRYSDT RRLHPLSTKN LSLEMAIDTE
SDLLEPLRSR ADLIIDTSEM SVHELAEMLR TRLLGKRERE LTMVFESFGF KHGIPIDADY
VFDVRFLPNP HWDPKLRPMT GLDRPVAAFL DRHTEVHNFI YQTRSYLELW LPMLETNNRS
YLTVAIGCTG GKHRSVYVAE QLADYFRSRG KNVQSRHRTL EKRK