ID   PROQ_YERPS              Reviewed;         237 AA.
AC   Q669V5;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=RNA chaperone ProQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   Name=proQ {ECO:0000255|HAMAP-Rule:MF_00749}; OrderedLocusNames=YPTB2377;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH21615.1; -; Genomic_DNA.
DR   RefSeq; WP_002210849.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q669V5; -.
DR   SMR; Q669V5; -.
DR   EnsemblBacteria; CAH21615; CAH21615; YPTB2377.
DR   GeneID; 66841191; -.
DR   KEGG; ypo:BZ17_78; -.
DR   KEGG; yps:YPTB2377; -.
DR   PATRIC; fig|273123.14.peg.83; -.
DR   OMA; WRYLKGV; -.
DR   Proteomes; UP000001011; 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; 2.
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..237
FT                   /note="RNA chaperone ProQ"
FT                   /id="PRO_0000303107"
FT   REGION          106..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..155
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   237 AA;  26498 MW;  F64F645A778F188F CRC64;
     MENQPKLNSS KEVIAFLAER FPLCFTAEGE ARPLKIGIFQ DLVERVQGEE NLSKTQLRSA
     LRLYTSSWRY LYGVKVGAER VDLDGNPCGV LEEQHVEHAR KQLEEAKARV QAQRAEQQAK
     KREAAIAAGE TPEPRRPRPA GKKPAPRREA GAAPENRKPR QSPRPQQVRP PRPQVEENQP
     RPVPVTDISK LQIGQEIKVR AGKSAMDATV LEIAKDGVRV QLSSGLAMIV RAEHLQF