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Database: UniProt
Entry: H2IU72_RAHAC
LinkDB: H2IU72_RAHAC
Original site: H2IU72_RAHAC 
ID   H2IU72_RAHAC            Unreviewed;       284 AA.
AC   H2IU72;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=RNase adapter protein RapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN   Name=rapZ {ECO:0000256|HAMAP-Rule:MF_00636};
GN   OrderedLocusNames=Rahaq2_4084 {ECO:0000313|EMBL:AEX53854.1};
OS   Rahnella aquatilis (strain ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 /
OS   NCIMB 13365 / CIP 78.65).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Rahnella.
OX   NCBI_TaxID=745277 {ECO:0000313|EMBL:AEX53854.1, ECO:0000313|Proteomes:UP000009010};
RN   [1] {ECO:0000313|EMBL:AEX53854.1, ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RX   PubMed=22582378; DOI=10.1128/JB.00380-12;
RA   Martinez R.J., Bruce D., Detter C., Goodwin L.A., Han J., Han C.S.,
RA   Held B., Land M.L., Mikhailova N., Nolan M., Pennacchio L., Pitluck S.,
RA   Tapia R., Woyke T., Sobecky P.A.;
RT   "Complete Genome Sequence of Rahnella aquatilis CIP 78.65.";
RL   J. Bacteriol. 194:3020-3021(2012).
RN   [2] {ECO:0000313|Proteomes:UP000009010}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33071 / DSM 4594 / JCM 1683 / NBRC 105701 / NCIMB 13365 /
RC   CIP 78.65 {ECO:0000313|Proteomes:UP000009010};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Held B., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Sobecky P.,
RA   Martinez R., Woyke T.;
RT   "Complete sequence of chromosome of Rahnella aquatilis CIP 78.65.";
RL   Submitted (JAN-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}.
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DR   EMBL; CP003244; AEX53854.1; -; Genomic_DNA.
DR   RefSeq; WP_013577261.1; NZ_JMPO01000127.1.
DR   AlphaFoldDB; H2IU72; -.
DR   STRING; 745277.Rahaq2_4084; -.
DR   GeneID; 61514030; -.
DR   KEGG; raq:Rahaq2_4084; -.
DR   PATRIC; fig|745277.3.peg.3919; -.
DR   eggNOG; COG1660; Bacteria.
DR   HOGENOM; CLU_059558_1_1_6; -.
DR   OrthoDB; 9784461at2; -.
DR   Proteomes; UP000009010; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; 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   Kinase {ECO:0000313|EMBL:AEX53854.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009010};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00636};
KW   Transferase {ECO:0000313|EMBL:AEX53854.1}.
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;  32522 MW;  989E2CC3BCAC4D20 CRC64;
     MVLMIVSGRS GSGKSVALRA LEDMGFYCVD NLPVVLLPQL AQTLVERNTS AAVSIDVRNM
     PETPEVYEYA MSQLPESFSP QLLFLDADRN TLIRRYSDTR RLHPLSSKNL SLESAIDEEA
     DLLEPLRSSA DLIIDTSEMS VHELAEMLRT RLLGKREREL TMVFESFGFK HGIPIDADYV
     FDVRFLPNPH WDPKLRPMTG LDKPVAAFLD RHTEVHNFIY QTRSYLEQWL PMLETNNRSY
     LTVAIGCTGG KHRSVYIAEQ LADYFRSRGK NVQSRHRTLE KRKS
//
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