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Database: UniProt
Entry: B4RK18_NEIG2
LinkDB: B4RK18_NEIG2
Original site: B4RK18_NEIG2 
ID   B4RK18_NEIG2            Unreviewed;        91 AA.
AC   B4RK18;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   RecName: Full=RNA-binding protein Hfq {ECO:0000256|HAMAP-Rule:MF_00436};
GN   Name=hfq {ECO:0000256|HAMAP-Rule:MF_00436};
GN   OrderedLocusNames=NGK_0479 {ECO:0000313|EMBL:ACF29170.1};
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=521006 {ECO:0000313|EMBL:ACF29170.1, ECO:0000313|Proteomes:UP000002564};
RN   [1] {ECO:0000313|EMBL:ACF29170.1, ECO:0000313|Proteomes:UP000002564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945 {ECO:0000313|EMBL:ACF29170.1,
RC   ECO:0000313|Proteomes:UP000002564};
RX   PubMed=18586945; DOI=10.1128/JB.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
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; CP001050; ACF29170.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4RK18; -.
DR   KEGG; ngk:NGK_0479; -.
DR   HOGENOM; CLU_113688_2_2_4; -.
DR   Proteomes; UP000002564; Chromosome.
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          4..64
FT                   /note="Sm"
FT                   /evidence="ECO:0000259|PROSITE:PS52002"
FT   REGION          69..91
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   91 AA;  10167 MW;  11F727D0A1D72F2B CRC64;
     MLQDPFLNAL RKEHVPVSIY LVNGIKLQGQ VESFDQYVVL LRNTSVTQMV YKHAISTIVP
     ARSVNLQHEN KPQAAPASTL VQVETVQQPA E
//
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