ID A0A085JQC6_9GAMM Unreviewed; 284 AA.
AC A0A085JQC6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN Name=yhbJ {ECO:0000313|EMBL:KFD22672.1};
GN Synonyms=rapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN ORFNames=GTPT_0251 {ECO:0000313|EMBL:KFD22672.1};
OS Tatumella ptyseos ATCC 33301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Tatumella.
OX NCBI_TaxID=1005995 {ECO:0000313|EMBL:KFD22672.1, ECO:0000313|Proteomes:UP000028602};
RN [1] {ECO:0000313|EMBL:KFD22672.1, ECO:0000313|Proteomes:UP000028602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33301 {ECO:0000313|EMBL:KFD22672.1,
RC ECO:0000313|Proteomes:UP000028602};
RA Plunkett G.III., Neeno-Eckwall E.C., Glasner J.D., Perna N.T.;
RT "ATOL: Assembling a taxonomically balanced genome-scale reconstruction of
RT the evolutionary history of the Enterobacteriaceae.";
RL Submitted (MAY-2014) 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:KFD22672.1}.
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DR EMBL; JMPR01000004; KFD22672.1; -; Genomic_DNA.
DR RefSeq; WP_025903821.1; NZ_JMPR01000004.1.
DR AlphaFoldDB; A0A085JQC6; -.
DR eggNOG; COG1660; Bacteria.
DR OrthoDB; 9784461at2; -.
DR Proteomes; UP000028602; 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, ECO:0000313|EMBL:KFD22672.1};
KW GTP-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW Reference proteome {ECO:0000313|Proteomes:UP000028602};
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; 32708 MW; 654E85C6E0BF4FBA CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVDLLPEL ANSLAKQDIS AAVSIDVRNM
PESPEIFENA FNRLSDKFTP QLLFLDADRN TLIRRYSDTR RLHPLSGRNL SLESAIDEES
DLLEPLRSRA DLIIDTSEMS VHELAEMLRA RLLGKREREL TIVFESFGFK YGIPIDADYV
FDVRFLPNPH WDPTLRPFTG LDRPVIEFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
LTVAIGCTGG KHRSVYIAEQ LADYFRSRGK NVQSRHRTLE KKRK
//
