HFQ_XANCP
ID HFQ_XANCP Reviewed; 92 AA.
AC Q8P9X7;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
GN Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; OrderedLocusNames=XCC1716;
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
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; AE008922; AAM41010.1; -; Genomic_DNA.
DR RefSeq; NP_637086.1; NC_003902.1.
DR RefSeq; WP_011036893.1; NC_003902.1.
DR AlphaFoldDB; Q8P9X7; -.
DR SMR; Q8P9X7; -.
DR STRING; 340.xcc-b100_2543; -.
DR EnsemblBacteria; AAM41010; AAM41010; XCC1716.
DR GeneID; 58013730; -.
DR KEGG; xcc:XCC1716; -.
DR PATRIC; fig|190485.4.peg.1831; -.
DR eggNOG; COG1923; Bacteria.
DR HOGENOM; CLU_113688_2_0_6; -.
DR OMA; QQMVYKH; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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 3: Inferred from homology;
KW Reference proteome; RNA-binding; Stress response.
FT CHAIN 1..92
FT /note="RNA-binding protein Hfq"
FT /id="PRO_0000095672"
FT REGION 72..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 92 AA; 10203 MW; 265E445DE244DE7E CRC64;
MAKGQSLQDP FLNALRRERV PVSVYLVNGI KLQGTIESFD QFVVLLRNTV SQMVYKHAIS
TVVPARNVRV GPGGGYVQSN ENNQAEDDDV EQ
