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 27-MAR-2024, entry version 85.
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; Pseudomonadota; 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}.
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DR EMBL; AM421808; CAM09993.1; -; Genomic_DNA.
DR RefSeq; WP_002236839.1; NC_008767.1.
DR PDB; 7OG8; X-ray; 1.40 A; A=5-72.
DR PDBsum; 7OG8; -.
DR AlphaFoldDB; A1KT11; -.
DR SMR; A1KT11; -.
DR GeneID; 83546234; -.
DR KEGG; nmc:NMC0702; -.
DR HOGENOM; CLU_113688_2_2_4; -.
DR Proteomes; UP000002286; Chromosome.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd01716; Hfq; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR HAMAP; MF_00436; Hfq; 1.
DR InterPro; IPR005001; Hfq.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR047575; Sm.
DR NCBIfam; TIGR02383; Hfq; 1.
DR PANTHER; PTHR34772; RNA-BINDING PROTEIN HFQ; 1.
DR PANTHER; PTHR34772:SF1; RNA-BINDING PROTEIN HFQ; 1.
DR Pfam; PF17209; Hfq; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS52002; SM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; RNA-binding; Stress response.
FT CHAIN 1..97
FT /note="RNA-binding protein Hfq"
FT /id="PRO_1000025921"
FT DOMAIN 10..70
FT /note="Sm"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT REGION 75..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 9..19
FT /evidence="ECO:0007829|PDB:7OG8"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:7OG8"
FT STRAND 32..40
FT /evidence="ECO:0007829|PDB:7OG8"
FT STRAND 42..48
FT /evidence="ECO:0007829|PDB:7OG8"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:7OG8"
FT HELIX 58..60
FT /evidence="ECO:0007829|PDB:7OG8"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:7OG8"
SQ SEQUENCE 97 AA; 10811 MW; AC50A6BD58C10EA1 CRC64;
MTAKGQMLQD PFLNALRKEH VPVSIYLVNG IKLQGQVESF DQYVVLLRNT SVTQMVYKHA
ISTIVPARSV NLQHENRPQA APASTLVQVE TVQQPAE
//
