ID S9QXT2_9RHOB Unreviewed; 611 AA.
AC S9QXT2;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000256|HAMAP-Rule:MF_00436};
GN Name=hfq {ECO:0000256|HAMAP-Rule:MF_00436};
GN ORFNames=ruthe_00970 {ECO:0000313|EMBL:EPX86161.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX86161.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX86161.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX86161.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
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:0000256|HAMAP-Rule:MF_00436}.
CC -!- SUBUNIT: Homohexamer. {ECO:0000256|HAMAP-Rule:MF_00436}.
CC -!- SIMILARITY: Belongs to the Hfq family. {ECO:0000256|HAMAP-
CC Rule:MF_00436}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPX86161.1}.
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DR EMBL; AOLV01000010; EPX86161.1; -; Genomic_DNA.
DR AlphaFoldDB; S9QXT2; -.
DR SMR; S9QXT2; -.
DR STRING; 1123069.ruthe_00970; -.
DR PATRIC; fig|1123069.3.peg.941; -.
DR HOGENOM; CLU_000445_0_6_5; -.
DR Proteomes; UP000015346; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00009; AAA; 1.
DR CDD; cd01716; Hfq; 1.
DR CDD; cd17550; REC_NtrX-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.30.30.100; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00436; Hfq; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR005001; Hfq.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR InterPro; IPR047575; Sm.
DR NCBIfam; TIGR02383; Hfq; 1.
DR PANTHER; PTHR32071:SF17; TRANSCRIPTIONAL REGULATOR (NTRC FAMILY); 1.
DR PANTHER; PTHR32071; TRANSCRIPTIONAL REGULATORY PROTEIN; 1.
DR Pfam; PF17209; Hfq; 1.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
DR PROSITE; PS52002; SM; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00436};
KW Stress response {ECO:0000256|HAMAP-Rule:MF_00436}.
FT DOMAIN 3..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 141..366
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000259|PROSITE:PS50045"
FT DOMAIN 544..604
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 440..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 52
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 611 AA; 66897 MW; ED6AC285557E6BC1 CRC64;
MGDILITDDE RDIRELISDI LRDEGYTTRL AGTSEQCMAE IAREVPALMI LDIWLKDSRM
DGIDILKTMK REHPEVPIII ISGHGNIEIA VAAIKQGAYD FIEKPFNIEQ LLVVIRRAME
TSRLRRENQA LKRGGAQKTE MLGDSPAFRS LKAQLEKVTK SNGRVMLTGE PGSGKETAAR
WIHAHSNRAS GPFVVVSSAS IEPERFEEVL FGRESAGKGI EKGLLEQAHG GIIYFDEVAD
MPLGTQSKIL RVLVDQQFVR VGGTEKIHVD MRVISSTNRD LKAAIAAGTF RQELYHRLNV
VPIAVPSLGD RREDIPLLAE HFIQLLNKTQ GLPLRRLGED ARALLQTMHW PGNVRQLRNV
IERVLILGEP TGDITARELP SMDESAPDDN RVVLSGGLAT LPLREARELF EKEYLLTQIN
RFGGNISRTA AFVGSGAVGA PSQAQVSGRR DGPQGHAAPG LCRGGMMASE DNPAPRRTLG
IVRPAASAQP IPGKPATAMP ENMLRGLESP PVSRHSDAEG DGPSQGRKTK AGAGMAEGKQ
NLQDAFLNHV RKTKVPVTIF LINGVKLQGV ITWFDSFCVL LRRDGQSQLV YKSAISTIMP
SQPVNLYDGD D
//
