ID B9VV05_NEIME Unreviewed; 97 AA.
AC B9VV05;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=RNA-binding protein Hfq {ECO:0000256|HAMAP-Rule:MF_00436};
GN Name=hfq {ECO:0000256|HAMAP-Rule:MF_00436};
GN ORFNames=COH52_02035 {ECO:0000313|EMBL:RQK80999.1}, LD10_10560
GN {ECO:0000313|EMBL:KQB49684.1};
OS Neisseria meningitidis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=487 {ECO:0000313|EMBL:ACM66930.1};
RN [1] {ECO:0000313|EMBL:ACM66930.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=H44/76 {ECO:0000313|EMBL:ACM66930.1};
RA Pannekoek Y., Huis in 't Veld R., Hopman C.T.P., Langerak A.A.J.,
RA Speijer D., van der Ende A.;
RT "Molecular characterization and identification of proteins regulated by Hfq
RT in Neisseria meningitidis.";
RL FEMS Microbiol. Lett. 294:216-224(2009).
RN [2] {ECO:0000313|EMBL:KQB49684.1, ECO:0000313|Proteomes:UP000050419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12611 {ECO:0000313|EMBL:KQB49684.1,
RC ECO:0000313|Proteomes:UP000050419};
RA Mustapha M., Marsh J.W., Fernandez J.O., de Lemos A.P., Wang X.,
RA Mayer L.W., Lawrence J.G., Hiller N.L., Harrison L.H.;
RT "Capsular Switching and Global Spread of Hypervirulent Serogroup W, ST-11
RT Neisseria meningitidis.";
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:RQK80999.1, ECO:0000313|Proteomes:UP000283666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=INS-Nm1012 {ECO:0000313|EMBL:RQK80999.1,
RC ECO:0000313|Proteomes:UP000283666};
RA Duarte C., Gabastou J.M., Moreno J.;
RT "Phenotypic and genotypic characterization of Colombian isolates of
RT Neisseria meningitidis recovered from invasive disease.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; FJ606876; ACM66930.1; -; Genomic_DNA.
DR EMBL; JRFI01000542; KQB49684.1; -; Genomic_DNA.
DR EMBL; NWZY01000003; RQK80999.1; -; Genomic_DNA.
DR RefSeq; WP_002236839.1; NZ_WSPB01000066.1.
DR GeneID; 83546234; -.
DR PATRIC; fig|487.1143.peg.903; -.
DR OMA; QQMVYKH; -.
DR Proteomes; UP000050419; Unassembled WGS sequence.
DR Proteomes; UP000283666; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW Rule:MF_00436};
KW Stress response {ECO:0000256|ARBA:ARBA00023016, ECO:0000256|HAMAP-
KW Rule:MF_00436}.
FT DOMAIN 10..70
FT /note="Sm"
FT /evidence="ECO:0000259|PROSITE:PS52002"
FT REGION 75..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 97 AA; 10811 MW; AC50A6BD58C10EA1 CRC64;
MTAKGQMLQD PFLNALRKEH VPVSIYLVNG IKLQGQVESF DQYVVLLRNT SVTQMVYKHA
ISTIVPARSV NLQHENRPQA APASTLVQVE TVQQPAE
//
