ID HFQ_YEREN Reviewed; 101 AA.
AC Q56928;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 13-SEP-2023, entry version 103.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
DE AltName: Full=Yersinia multiple regulator;
DE AltName: Full=Yersinia regulator for pleiotropic phenotype;
GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; Synonyms=ymr, yrp;
OS Yersinia enterocolitica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=630;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=86-8;
RX PubMed=8825090; DOI=10.1111/j.1365-2958.1995.18050859.x;
RA Nakao H., Watanabe H., Nakayama S., Takeda T.;
RT "yst gene expression in Yersinia enterocolitica is positively regulated by
RT a chromosomal region that is highly homologous to Escherichia coli host
RT factor 1 gene (hfq).";
RL Mol. Microbiol. 18:859-865(1995).
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). Positively regulates the expression of the yst gene for
CC heat-stable enterotoxin (Y-ST). {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; D28762; BAA05952.1; -; Genomic_DNA.
DR PIR; S70842; S70842.
DR RefSeq; WP_004392473.1; NZ_UHIX01000001.1.
DR AlphaFoldDB; Q56928; -.
DR SMR; Q56928; -.
DR STRING; 1443113.LC20_04803; -.
DR GeneID; 77329802; -.
DR eggNOG; COG1923; Bacteria.
DR OMA; QQMVYKH; -.
DR PHI-base; PHI:6403; -.
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 3: Inferred from homology;
KW RNA-binding; Stress response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..101
FT /note="RNA-binding protein Hfq"
FT /id="PRO_0000095608"
FT DOMAIN 9..68
FT /note="Sm"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01346"
FT REGION 63..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 101 AA; 11143 MW; 767D3C06B221441D CRC64;
MAKGQSLQDP FLNALRRERV PVSIYLVNGI KLQGQVESFD QFVILLKNTV SQMVYKHAIS
TVVPSRPVSH HSNNPSGSTN NYHGSNPSAP QQPQQDSDDA E
//
