HFQ_SALTI
ID HFQ_SALTI Reviewed; 102 AA.
AC P0A1R1; Q56059;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN OrderedLocusNames=STY4718, t4412;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD06838.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71861.1; -; Genomic_DNA.
DR RefSeq; NP_458797.1; NC_003198.1.
DR RefSeq; WP_001051875.1; NZ_WSUR01000012.1.
DR AlphaFoldDB; P0A1R1; -.
DR SMR; P0A1R1; -.
DR STRING; 220341.16505488; -.
DR EnsemblBacteria; AAO71861; AAO71861; t4412.
DR KEGG; stt:t4412; -.
DR KEGG; sty:STY4718; -.
DR PATRIC; fig|220341.7.peg.4819; -.
DR eggNOG; COG1923; Bacteria.
DR HOGENOM; CLU_113688_2_1_6; -.
DR OMA; QQMVYKH; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..102
FT /note="RNA-binding protein Hfq"
FT /id="PRO_0000095605"
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"
SQ SEQUENCE 102 AA; 11133 MW; E53C7460172CF04F CRC64;
MAKGQSLQDP FLNALRRERV PVSIYLVNGI KLQGQIESFD QFVILLKNTV SQMVYKHAIS
TVVPSRPVSH HSNNAGGGAS NNYHHGSNAQ GSTAQQDSEE TE