HFQ_SALTY
ID HFQ_SALTY Reviewed; 102 AA.
AC P0A1R0; Q56059;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=STM4361;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=8682778; DOI=10.1128/jb.178.13.3763-3770.1996;
RA Brown L., Elliott T.;
RT "Efficient translation of the RpoS sigma factor in Salmonella typhimurium
RT requires host factor I, an RNA-binding protein encoded by the hfq gene.";
RL J. Bacteriol. 178:3763-3770(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RX PubMed=17163975; DOI=10.1111/j.1365-2958.2006.05489.x;
RA Sittka A., Pfeiffer V., Tedin K., Vogel J.;
RT "The RNA chaperone Hfq is essential for the virulence of Salmonella
RT typhimurium.";
RL Mol. Microbiol. 63:193-217(2007).
RN [4]
RP EFFECT OF SPACE FLIGHT CONDITIONS ON HFQ.
RC STRAIN=SL1344;
RX PubMed=17901201; DOI=10.1073/pnas.0707155104;
RA Wilson J.W., Ott C.M., Honer zu Bentrup K., Ramamurthy R., Quick L.,
RA Porwollik S., Cheng P., McClelland M., Tsaprailis G., Radabaugh T.,
RA Hunt A., Fernandez D., Richter E., Shah M., Kilcoyne M., Joshi L.,
RA Nelman-Gonzalez M., Hing S., Parra M., Dumars P., Norwood K., Bober R.,
RA Devich J., Ruggles A., Goulart C., Rupert M., Stodieck L., Stafford P.,
RA Catella L., Schurr M.J., Buchanan K., Morici L., McCracken J., Allen P.,
RA Baker-Coleman C., Hammond T., Vogel J., Nelson R., Pierson D.L.,
RA Stefanyshyn-Piper H.M., Nickerson C.A.;
RT "Space flight alters bacterial gene expression and virulence and reveals a
RT role for global regulator Hfq.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:16299-16304(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 (By
CC similarity). Plays a central regulatory role in the microbial response
CC to space flight conditions. Is essential for virulence and is required
CC for efficient invasion of non-phagocytic cells. {ECO:0000255|HAMAP-
CC Rule:MF_00436, ECO:0000269|PubMed:17163975}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_00436}.
CC -!- INTERACTION:
CC P0A1R0; P0A1R0: hfq; NbExp=2; IntAct=EBI-15935266, EBI-15935266;
CC -!- DISRUPTION PHENOTYPE: Cells display drastically reduced virulence in
CC vitro and in vivo. Mice infected with the deletion mutant show no signs
CC of illness during the course of the experiment. This suggests that the
CC mutation results in defects in either invasion of intestinal epithelial
CC cells, macrophage survival, or both. {ECO:0000269|PubMed:17163975}.
CC -!- MISCELLANEOUS: Hfq expression was decreased during the space flight and
CC expression of 64 genes of the hfq regulon was altered. Likewise,
CC several small RNAs that interact with hfq were differentially regulated
CC during the flight (PubMed:17901201). {ECO:0000305|PubMed:17901201}.
CC -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000255|HAMAP-
CC Rule:MF_00436}.
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DR EMBL; U48735; AAA99108.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL23181.1; -; Genomic_DNA.
DR RefSeq; NP_463222.1; NC_003197.2.
DR RefSeq; WP_001051875.1; NC_003197.2.
DR PDB; 2YLB; X-ray; 1.15 A; A/B/C/D/E/F=1-72.
DR PDB; 2YLC; X-ray; 1.30 A; A=1-72.
DR PDBsum; 2YLB; -.
DR PDBsum; 2YLC; -.
DR AlphaFoldDB; P0A1R0; -.
DR SMR; P0A1R0; -.
DR DIP; DIP-59697N; -.
DR STRING; 99287.STM4361; -.
DR PaxDb; P0A1R0; -.
DR EnsemblBacteria; AAL23181; AAL23181; STM4361.
DR GeneID; 1255887; -.
DR KEGG; stm:STM4361; -.
DR PATRIC; fig|99287.12.peg.4585; -.
DR HOGENOM; CLU_113688_2_1_6; -.
DR OMA; QQMVYKH; -.
DR PhylomeDB; P0A1R0; -.
DR BioCyc; SENT99287:STM4361-MON; -.
DR PHI-base; PHI:2687; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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 3D-structure; Reference proteome; RNA-binding; Stress response; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..102
FT /note="RNA-binding protein Hfq"
FT /id="PRO_0000095606"
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"
FT CONFLICT 13..14
FT /note="NA -> KP (in Ref. 1; AAA99108)"
FT /evidence="ECO:0000305"
FT HELIX 8..18
FT /evidence="ECO:0007829|PDB:2YLB"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:2YLB"
FT STRAND 31..39
FT /evidence="ECO:0007829|PDB:2YLB"
FT STRAND 41..55
FT /evidence="ECO:0007829|PDB:2YLB"
FT HELIX 56..58
FT /evidence="ECO:0007829|PDB:2YLB"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:2YLB"
SQ SEQUENCE 102 AA; 11133 MW; E53C7460172CF04F CRC64;
MAKGQSLQDP FLNALRRERV PVSIYLVNGI KLQGQIESFD QFVILLKNTV SQMVYKHAIS
TVVPSRPVSH HSNNAGGGAS NNYHHGSNAQ GSTAQQDSEE TE
