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HFQ_PHOPR
ID   HFQ_PHOPR               Reviewed;          85 AA.
AC   Q9EYZ5;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   25-MAY-2022, entry version 109.
DE   RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN   Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=PBPRA3350;
OS   Photobacterium profundum (strain SS9).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=298386;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1253 / SS9;
RX   PubMed=15746425; DOI=10.1126/science.1103341;
RA   Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M.,
RA   Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C.,
RA   Bartlett D.H., Valle G.;
RT   "Life at depth: Photobacterium profundum genome sequence and expression
RT   analysis.";
RL   Science 307:1459-1461(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-64.
RA   Bidle K.A., Bartlett D.H.;
RT   "An RNA arbitrarily primed PCR survey of genes regulated at low and high
RT   pressure by ToxR in the marine bacterium Photobacterium profundum SS9.";
RL   Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: RNA chaperone that binds small regulatory RNA (sRNAs) and
CC       mRNAs to facilitate mRNA translational regulation in response to
CC       envelope stress, environmental stress and changes in metabolite
CC       concentrations. Also binds with high specificity to tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_00436}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00436}.
CC   -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000255|HAMAP-
CC       Rule:MF_00436}.
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DR   EMBL; CR378673; CAG21648.1; -; Genomic_DNA.
DR   EMBL; AF307979; AAG34558.1; -; Genomic_DNA.
DR   RefSeq; WP_011219894.1; NC_006370.1.
DR   AlphaFoldDB; Q9EYZ5; -.
DR   SMR; Q9EYZ5; -.
DR   STRING; 298386.PBPRA3350; -.
DR   EnsemblBacteria; CAG21648; CAG21648; PBPRA3350.
DR   KEGG; ppr:PBPRA3350; -.
DR   eggNOG; COG1923; Bacteria.
DR   HOGENOM; CLU_113688_2_2_6; -.
DR   OMA; QQMVYKH; -.
DR   OrthoDB; 1989988at2; -.
DR   Proteomes; UP000000593; Chromosome 1.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR   CDD; cd01716; Hfq; 1.
DR   HAMAP; MF_00436; Hfq; 1.
DR   InterPro; IPR005001; Hfq.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   PANTHER; PTHR34772; PTHR34772; 1.
DR   Pfam; PF17209; Hfq; 1.
DR   SUPFAM; SSF50182; SSF50182; 1.
DR   TIGRFAMs; TIGR02383; Hfq; 1.
PE   3: Inferred from homology;
KW   Reference proteome; RNA-binding; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..85
FT                   /note="RNA-binding protein Hfq"
FT                   /id="PRO_0000095659"
FT   REGION          66..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..85
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        63..64
FT                   /note="VP -> IR (in Ref. 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   85 AA;  9649 MW;  82E219743D5017C8 CRC64;
     MAKGQSLQDP FLNALRRERI PVSIYLVNGI KLQGQIESFD QFVILLKNTV NQMVYKHAIS
     TVVPARPVNH HHASDRPATL EKTEE
 
 
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