ID   PROQ_ECO24              Reviewed;         232 AA.
AC   A7ZMV4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=RNA chaperone ProQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   Name=proQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   OrderedLocusNames=EcE24377A_2060;
OS   Escherichia coli O139:H28 (strain E24377A / ETEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=331111;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E24377A / ETEC;
RX   PubMed=18676672; DOI=10.1128/jb.00619-08;
RA   Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F.,
RA   Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R.,
RA   Henderson I.R., Sperandio V., Ravel J.;
RT   "The pangenome structure of Escherichia coli: comparative genomic analysis
RT   of E. coli commensal and pathogenic isolates.";
RL   J. Bacteriol. 190:6881-6893(2008).
CC   -!- FUNCTION: RNA chaperone with significant RNA binding, RNA strand
CC       exchange and RNA duplexing activities. May regulate ProP activity
CC       through an RNA-based, post-transcriptional mechanism.
CC       {ECO:0000255|HAMAP-Rule:MF_00749}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00749}.
CC   -!- SIMILARITY: Belongs to the ProQ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00749}.
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DR   EMBL; CP000800; ABV20818.1; -; Genomic_DNA.
DR   RefSeq; WP_000431363.1; NC_009801.1.
DR   AlphaFoldDB; A7ZMV4; -.
DR   SMR; A7ZMV4; -.
DR   EnsemblBacteria; ABV20818; ABV20818; EcE24377A_2060.
DR   KEGG; ecw:EcE24377A_2060; -.
DR   HOGENOM; CLU_113254_0_0_6; -.
DR   OMA; WRYLKGV; -.
DR   Proteomes; UP000001122; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033592; F:RNA strand annealing activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0034057; F:RNA strand-exchange activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IEA:InterPro.
DR   Gene3D; 1.10.1710.10; -; 1.
DR   HAMAP; MF_00749; ProQ; 1.
DR   InterPro; IPR023529; ProQ.
DR   InterPro; IPR016103; ProQ/FinO.
DR   InterPro; IPR036442; ProQ/FinO_sf.
DR   InterPro; IPR035236; ProQ_C.
DR   PANTHER; PTHR38106; PTHR38106; 1.
DR   Pfam; PF04352; ProQ; 1.
DR   Pfam; PF17516; ProQ_C; 1.
DR   SMART; SM00945; ProQ; 1.
DR   SUPFAM; SSF48657; SSF48657; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; RNA-binding.
FT   CHAIN           1..232
FT                   /note="RNA chaperone ProQ"
FT                   /id="PRO_1000062181"
FT   REGION          105..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   232 AA;  25803 MW;  1DDF98F570C09248 CRC64;
     MENQPKLNSS KEVIAFLAER FPHCFSAEGE ARPLKIGIFQ DLVDRVAGEM NLSKTQLRSA
     LRLYTSSWRY LYGVKPGATR VDLDGNPCGE LDEQHVEHAR KQLEEAKARV QAQRAEQQAK
     KREAAAAAGE KEDAPPRERK PRPTTPRRKE GAERKPRAQK PVEKAPKTVK APREEQHTPV
     SDISALTVGQ ALKVKAGQNA MDATVLEITK DGVRVQLNSG MSLIVRAEHL VF