ID H5UZH8_ATLHE Unreviewed; 284 AA.
AC H5UZH8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=RNase adapter protein RapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN Name=rapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN Synonyms=yhbJ {ECO:0000313|EMBL:GAB51136.1};
GN ORFNames=EH105704_02_01650 {ECO:0000313|EMBL:GAB51136.1};
OS Atlantibacter hermannii NBRC 105704.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Atlantibacter.
OX NCBI_TaxID=1115512 {ECO:0000313|EMBL:GAB51136.1, ECO:0000313|Proteomes:UP000010297};
RN [1] {ECO:0000313|EMBL:GAB51136.1, ECO:0000313|Proteomes:UP000010297}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 105704 {ECO:0000313|EMBL:GAB51136.1,
RC ECO:0000313|Proteomes:UP000010297};
RA Yoshida I., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Escherichia hermannii NBRC 105704.";
RL Submitted (FEB-2012) 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:GAB51136.1}.
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DR EMBL; BAFF01000002; GAB51136.1; -; Genomic_DNA.
DR RefSeq; WP_002434202.1; NZ_BAFF01000002.1.
DR AlphaFoldDB; H5UZH8; -.
DR GeneID; 75062239; -.
DR eggNOG; COG1660; Bacteria.
DR Proteomes; UP000010297; 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 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:UP000010297};
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; 32481 MW; CEE9D08C2B714CF2 CRC64;
MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPDL ARTLSDSHIS AAVSIDVRNM
PESPEIFEQA MSNLPDTFSP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLESAIDQES
DLLEPLRSRA DLIVDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
FDVRFLPNPH WDPKLRPMTG LDKPVAAFLD RHTEVHNFIY QTRSYLELWL PMLETNNRSY
LTVAIGCTGG KHRSVYIAEQ LADYFRSRGK NVQSRHRTLE KRKT
//
