ID   HFQ_PECCC               Reviewed;          99 AA.
AC   Q9ZI76;
DT   29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=RNA-binding protein Hfq {ECO:0000255|HAMAP-Rule:MF_00436};
DE   AltName: Full=Bacteriocin gene regulator;
GN   Name=hfq {ECO:0000255|HAMAP-Rule:MF_00436}; Synonyms=brg;
OS   Pectobacterium carotovorum subsp. carotovorum (Erwinia carotovora subsp.
OS   carotovora).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=CGE234-M403;
RX   PubMed=10074096; DOI=10.1128/jb.181.6.1953-1957.1999;
RA   Chuang D.-Y., Kyeremeh A.G., Gunji Y., Takahara Y., Ehara Y., Kikumoto T.;
RT   "Identification and cloning of an Erwinia carotovora subsp. carotovora
RT   bacteriocin regulator gene by insertional mutagenesis.";
RL   J. Bacteriol. 181:1953-1957(1999).
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 (By
CC       similarity). Involved in the regulation of the bacteriocin
CC       carotovoricin. {ECO:0000255|HAMAP-Rule:MF_00436,
CC       ECO:0000269|PubMed:10074096}.
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; AF039142; AAC98926.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZI76; -.
DR   SMR; Q9ZI76; -.
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   CHAIN           1..99
FT                   /note="RNA-binding protein Hfq"
FT                   /id="PRO_0000095637"
FT   REGION          64..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..99
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   99 AA;  10963 MW;  4E6DC43CB03C53AB CRC64;
     MVKGQSLQDP FLNALRRERV PVSIYLVNGI KLQGQIESFD QFVILLKNTV SQMVYKHAIS
     TVVPSRPVSH HSNNPGGSNN YHGSNTTAQQ QSQEADDAE