HFQ_THEMA
ID HFQ_THEMA Reviewed; 92 AA.
AC Q9WYZ6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 114.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=TM_0526;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD35611.1; -; Genomic_DNA.
DR PIR; D72366; D72366.
DR RefSeq; NP_228336.1; NC_000853.1.
DR PDB; 4Y91; X-ray; 2.66 A; A/B/C/D/E/F/G/H/I/J/K/L=1-92.
DR PDBsum; 4Y91; -.
DR AlphaFoldDB; Q9WYZ6; -.
DR SMR; Q9WYZ6; -.
DR STRING; 243274.THEMA_02045; -.
DR EnsemblBacteria; AAD35611; AAD35611; TM_0526.
DR KEGG; tma:TM0526; -.
DR PATRIC; fig|243274.5.peg.534; -.
DR eggNOG; COG1923; Bacteria.
DR InParanoid; Q9WYZ6; -.
DR OMA; QQMVYKH; -.
DR Proteomes; UP000008183; 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..92
FT /note="RNA-binding protein Hfq"
FT /id="PRO_0000095664"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:4Y91"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:4Y91"
FT STRAND 33..41
FT /evidence="ECO:0007829|PDB:4Y91"
FT STRAND 43..50
FT /evidence="ECO:0007829|PDB:4Y91"
FT STRAND 53..58
FT /evidence="ECO:0007829|PDB:4Y91"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:4Y91"
FT STRAND 62..69
FT /evidence="ECO:0007829|PDB:4Y91"
SQ SEQUENCE 92 AA; 10516 MW; 3E7D5B48E570C561 CRC64;
MALAEKFNLQ DRFLNHLRVN KIEVKVYLVN GFQTKGFIRS FDSYTVLLES GNQQSLIYKH
AISTIIPSSY VMLMPKKQET AQEAETSENE GS
