ID   HFQ_VIBCH               Reviewed;          87 AA.
AC   Q9KV11;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-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=VC_0347;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=15225327; DOI=10.1111/j.1365-2958.2004.04142.x;
RA   Ding Y., Davis B.M., Waldor M.K.;
RT   "Hfq is essential for Vibrio cholerae virulence and downregulates sigma
RT   expression.";
RL   Mol. Microbiol. 53:345-354(2004).
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 (By
CC       similarity). Essential for virulence in the suckling mouse model of
CC       cholera pathogenesis. {ECO:0000255|HAMAP-Rule:MF_00436,
CC       ECO:0000269|PubMed:15225327}.
CC   -!- DISRUPTION PHENOTYPE: A hfq deletion mutant cannot colonize the murine
CC       small intestine despite retaining the ability to produce the
CC       colonization factor TCP. Deletion of hfq does not impair production of
CC       the sigma factor RpoS. Expression and activity of the sigma factor
CC       sigma-E are dramatically increased in the hfq mutant.
CC       {ECO:0000269|PubMed:15225327}.
CC   -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000255|HAMAP-
CC       Rule:MF_00436}.
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DR   EMBL; AE003852; AAF93520.1; -; Genomic_DNA.
DR   PIR; C82334; C82334.
DR   RefSeq; NP_230001.1; NC_002505.1.
DR   RefSeq; WP_001051872.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KV11; -.
DR   SMR; Q9KV11; -.
DR   STRING; 243277.VC_0347; -.
DR   DNASU; 2615060; -.
DR   EnsemblBacteria; AAF93520; AAF93520; VC_0347.
DR   GeneID; 57991527; -.
DR   GeneID; 66940551; -.
DR   KEGG; vch:VC_0347; -.
DR   PATRIC; fig|243277.26.peg.324; -.
DR   eggNOG; COG1923; Bacteria.
DR   HOGENOM; CLU_113688_2_2_6; -.
DR   OMA; QQMVYKH; -.
DR   BioCyc; VCHO:VC0347-MON; -.
DR   PHI-base; PHI:704; -.
DR   Proteomes; UP000000584; Chromosome 1.
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   Reference proteome; RNA-binding; Stress response; Virulence.
FT   CHAIN           1..87
FT                   /note="RNA-binding protein Hfq"
FT                   /id="PRO_0000095666"
FT   REGION          65..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        72..87
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   87 AA;  9769 MW;  A7E4B6878A164DB0 CRC64;
     MAKGQSLQDP FLNALRRERI PVSIYLVNGI KLQGQIESFD QFVILLKNTV NQMVYKHAIS
     TVVPARPVSH HSGDRPASDR PAEKSEE