ID   HFQ_NEIMF               Reviewed;          97 AA.
AC   A1KT11;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN   Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=NMC0702;
OS   Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS   15464 / FAM18).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=272831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX   PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA   Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA   Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA   Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA   Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT   "Meningococcal genetic variation mechanisms viewed through comparative
RT   analysis of serogroup C strain FAM18.";
RL   PLoS Genet. 3:230-240(2007).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AM421808; CAM09993.1; -; Genomic_DNA.
DR   RefSeq; WP_002236839.1; NC_008767.1.
DR   AlphaFoldDB; A1KT11; -.
DR   SMR; A1KT11; -.
DR   PRIDE; A1KT11; -.
DR   EnsemblBacteria; CAM09993; CAM09993; NMC0702.
DR   KEGG; nmc:NMC0702; -.
DR   HOGENOM; CLU_113688_2_2_4; -.
DR   OMA; QQMVYKH; -.
DR   OrthoDB; 1989988at2; -.
DR   Proteomes; UP000002286; 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..97
FT                   /note="RNA-binding protein Hfq"
FT                   /id="PRO_1000025921"
FT   REGION          75..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   97 AA;  10811 MW;  AC50A6BD58C10EA1 CRC64;
     MTAKGQMLQD PFLNALRKEH VPVSIYLVNG IKLQGQVESF DQYVVLLRNT SVTQMVYKHA
     ISTIVPARSV NLQHENRPQA APASTLVQVE TVQQPAE