HFQ_AQUAE
ID HFQ_AQUAE Reviewed; 80 AA.
AC O66512;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=aq_108;
GN ORFNames=aq_108B;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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; AE000657; AAC06479.1; -; Genomic_DNA.
DR PIR; E70310; E70310.
DR RefSeq; NP_213072.1; NC_000918.1.
DR RefSeq; WP_010880010.1; NC_000918.1.
DR PDB; 5SZD; X-ray; 1.49 A; A/B/C/D/E/F/G/H/I/J/K/L=1-80.
DR PDB; 5SZE; X-ray; 1.50 A; A=1-80.
DR PDBsum; 5SZD; -.
DR PDBsum; 5SZE; -.
DR AlphaFoldDB; O66512; -.
DR SMR; O66512; -.
DR STRING; 224324.aq_108b; -.
DR EnsemblBacteria; AAC06479; AAC06479; aq_108b.
DR KEGG; aae:aq_108b; -.
DR PATRIC; fig|224324.8.peg.93; -.
DR eggNOG; COG1923; Bacteria.
DR HOGENOM; CLU_113688_0_2_0; -.
DR InParanoid; O66512; -.
DR OMA; QQMVYKH; -.
DR OrthoDB; 1989988at2; -.
DR Proteomes; UP000000798; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0043487; P:regulation of RNA stability; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0045974; P:regulation of translation, ncRNA-mediated; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..80
FT /note="RNA-binding protein Hfq"
FT /id="PRO_0000095612"
FT HELIX 4..16
FT /evidence="ECO:0007829|PDB:5SZD"
FT STRAND 19..24
FT /evidence="ECO:0007829|PDB:5SZD"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:5SZD"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:5SZD"
FT STRAND 49..54
FT /evidence="ECO:0007829|PDB:5SZD"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:5SZD"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:5SZD"
SQ SEQUENCE 80 AA; 9202 MW; 6E859985F4D53B4F CRC64;
MPYKLQESFL NTARKKRVKV SVYLVNGVRL QGRIRSFDLF TILLEDGKQQ TLVYKHAITT
IVPHERLEIE FEEAGVPGQG
