ID D4BK78_9ENTR Unreviewed; 284 AA.
AC D4BK78;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN ORFNames=CIT292_10695 {ECO:0000313|EMBL:EFE05721.1};
OS Citrobacter youngae ATCC 29220.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX NCBI_TaxID=500640 {ECO:0000313|EMBL:EFE05721.1, ECO:0000313|Proteomes:UP000003880};
RN [1] {ECO:0000313|EMBL:EFE05721.1, ECO:0000313|Proteomes:UP000003880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29220 {ECO:0000313|EMBL:EFE05721.1,
RC ECO:0000313|Proteomes:UP000003880};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EFE05721.1}.
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DR EMBL; ABWL02000026; EFE05721.1; -; Genomic_DNA.
DR RefSeq; WP_003025085.1; NZ_GG730303.1.
DR AlphaFoldDB; D4BK78; -.
DR GeneID; 73801044; -.
DR eggNOG; COG1660; Bacteria.
DR HOGENOM; CLU_059558_1_1_6; -.
DR Proteomes; UP000003880; Unassembled WGS sequence.
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 RNA-binding {ECO:0000256|HAMAP-Rule:MF_00636}.
FT REGION 266..284
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 284 AA; 32536 MW; 439528FFAD5857D9 CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPDL ARTLADRQIS AAVSIDVRNM
PESPEIFEQA MNNLPEGFSP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLESAIDKES
DLLEPLRSRA DLIVDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
FDVRFLPNPH WDPKLRPMTG LDRPVAAFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
LTVAIGCTGG KHRSVYIAEQ LADYFRSRGK NVQSRHRTLE KRKS
//
