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HFQ_ESCF3
ID   HFQ_ESCF3               Reviewed;         102 AA.
AC   B7LLV4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN   Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=EFER_4225;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928158; CAQ91644.1; -; Genomic_DNA.
DR   RefSeq; WP_001051883.1; NC_011740.1.
DR   AlphaFoldDB; B7LLV4; -.
DR   SMR; B7LLV4; -.
DR   EnsemblBacteria; CAQ91644; CAQ91644; EFER_4225.
DR   GeneID; 67414790; -.
DR   KEGG; efe:EFER_4225; -.
DR   HOGENOM; CLU_113688_2_1_6; -.
DR   OMA; QQMVYKH; -.
DR   OrthoDB; 1989988at2; -.
DR   BioCyc; EFER585054:EFER_RS21080-MON; -.
DR   Proteomes; UP000000745; Chromosome.
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   RNA-binding; Stress response.
FT   CHAIN           1..102
FT                   /note="RNA-binding protein Hfq"
FT                   /id="PRO_1000190331"
FT   REGION          63..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..102
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   102 AA;  11166 MW;  E47FA9B07A39304D CRC64;
     MAKGQSLQDP FLNALRRERV PVSIYLVNGI KLQGQIESFD QFVILLKNTV SQMVYKHAIS
     TVVPSRPVSH HSNNAGGGTS SNYHHGSSAQ NTSAQQDSEE TE
 
 
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