ID   PROQ_ECOLI              Reviewed;         232 AA.
AC   P45577; P56606;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1999, sequence version 2.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=RNA chaperone ProQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   Name=proQ {ECO:0000255|HAMAP-Rule:MF_00749}; Synonyms=yebJ, yobE, yoeC;
GN   OrderedLocusNames=b1831, JW5300;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND DISRUPTION
RP   PHENOTYPE.
RC   STRAIN=K12;
RX   PubMed=10049386; DOI=10.1128/jb.181.5.1537-1543.1999;
RA   Kunte H.J., Crane R.A., Culham D.E., Richmond D., Wood J.M.;
RT   "Protein ProQ influences osmotic activation of compatible solute
RT   transporter ProP in Escherichia coli K-12.";
RL   J. Bacteriol. 181:1537-1543(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA   Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA   Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA   Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA   Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA   Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA   Horiuchi T.;
RT   "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 40.1-50.0 min region on the linkage map.";
RL   DNA Res. 3:379-392(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-232.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=1856173; DOI=10.1128/jb.173.15.4799-4813.1991;
RA   Hara H., Yamamoto Y., Higashitani A., Suzuki H., Nishimura Y.;
RT   "Cloning, mapping, and characterization of the Escherichia coli prc gene,
RT   which is involved in C-terminal processing of penicillin-binding protein
RT   3.";
RL   J. Bacteriol. 173:4799-4813(1991).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-6, SUBCELLULAR LOCATION, AND DOMAIN.
RX   PubMed=15476391; DOI=10.1021/bi048561g;
RA   Smith M.N., Crane R.A., Keates R.A., Wood J.M.;
RT   "Overexpression, purification, and characterization of ProQ, a
RT   posttranslational regulator for osmoregulatory transporter ProP of
RT   Escherichia coli.";
RL   Biochemistry 43:12979-12989(2004).
RN   [7]
RP   IDENTIFICATION.
RX   PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA   Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT   "Detection of new genes in a bacterial genome using Markov models for three
RT   gene classes.";
RL   Nucleic Acids Res. 23:3554-3562(1995).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND DOMAIN.
RX   PubMed=17319698; DOI=10.1021/bi6023786;
RA   Smith M.N., Kwok S.C., Hodges R.S., Wood J.M.;
RT   "Structural and functional analysis of ProQ: an osmoregulatory protein of
RT   Escherichia coli.";
RL   Biochemistry 46:3084-3095(2007).
RN   [9]
RP   FUNCTION, RNA-BINDING, AND DOMAIN.
RX   PubMed=21381725; DOI=10.1021/bi101683a;
RA   Chaulk S.G., Smith Frieday M.N., Arthur D.C., Culham D.E., Edwards R.A.,
RA   Soo P., Frost L.S., Keates R.A., Glover J.N., Wood J.M.;
RT   "ProQ is an RNA chaperone that controls ProP levels in Escherichia coli.";
RL   Biochemistry 50:3095-3106(2011).
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, ECO:0000269|PubMed:21381725}.
CC   -!- INTERACTION:
CC       P45577; P0ACZ4: evgA; NbExp=3; IntAct=EBI-8767901, EBI-548694;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00749,
CC       ECO:0000269|PubMed:10049386, ECO:0000269|PubMed:15476391}.
CC   -!- DOMAIN: Contains an alpha-helical N-terminal domain (FinO-like) and a
CC       beta-sheet C-terminal domain (Hfq-like), connected by an unstructured
CC       linker. The FinO-like domain serves as a high-affinity RNA-binding
CC       domain, whereas the Hfq-like domain is largely responsible for RNA
CC       strand exchange and duplexing. {ECO:0000269|PubMed:15476391,
CC       ECO:0000269|PubMed:17319698, ECO:0000269|PubMed:21381725}.
CC   -!- DISRUPTION PHENOTYPE: Mutation reduces both the rate and the extent of
CC       ProP activation by an osmotic upshift, but does not impair
CC       transcription or translation of proP. {ECO:0000269|PubMed:10049386}.
CC   -!- SIMILARITY: Belongs to the ProQ family. {ECO:0000255|HAMAP-
CC       Rule:MF_00749}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20566.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAA20566.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; L48409; AAD41527.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC74901.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15639.2; -; Genomic_DNA.
DR   EMBL; D00674; BAA20566.1; ALT_SEQ; Genomic_DNA.
DR   PIR; G64944; G64944.
DR   RefSeq; WP_000431381.1; NZ_SSZK01000001.1.
DR   RefSeq; YP_026161.1; NC_000913.3.
DR   PDB; 5NBB; NMR; -; A=180-232.
DR   PDBsum; 5NBB; -.
DR   AlphaFoldDB; P45577; -.
DR   SMR; P45577; -.
DR   BioGRID; 4260696; 30.
DR   BioGRID; 853211; 40.
DR   DIP; DIP-10572N; -.
DR   IntAct; P45577; 43.
DR   STRING; 511145.b1831; -.
DR   jPOST; P45577; -.
DR   PaxDb; P45577; -.
DR   PRIDE; P45577; -.
DR   EnsemblBacteria; AAC74901; AAC74901; b1831.
DR   EnsemblBacteria; BAA15639; BAA15639; BAA15639.
DR   GeneID; 948950; -.
DR   KEGG; ecj:JW5300; -.
DR   KEGG; eco:b1831; -.
DR   PATRIC; fig|1411691.4.peg.419; -.
DR   EchoBASE; EB2707; -.
DR   eggNOG; COG3109; Bacteria.
DR   HOGENOM; CLU_113254_0_0_6; -.
DR   OMA; WRYLKGV; -.
DR   PhylomeDB; P45577; -.
DR   BioCyc; EcoCyc:EG12866-MON; -.
DR   PRO; PR:P45577; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0003730; F:mRNA 3'-UTR binding; IDA:EcoCyc.
DR   GO; GO:0003729; F:mRNA binding; IDA:EcoCyc.
DR   GO; GO:0033592; F:RNA strand annealing activity; IDA:EcoCyc.
DR   GO; GO:0034057; F:RNA strand-exchange activity; IDA:EcoCyc.
DR   GO; GO:0071475; P:cellular hyperosmotic salinity response; IMP:CAFA.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:EcoCyc.
DR   GO; GO:0007231; P:osmosensory signaling pathway; IMP:CAFA.
DR   GO; GO:1902836; P:positive regulation of proline import across plasma membrane; IMP:CAFA.
DR   GO; GO:0010608; P:post-transcriptional regulation of gene expression; IDA:EcoCyc.
DR   GO; GO:0044010; P:single-species biofilm formation; IMP:EcoCyc.
DR   DisProt; DP00377; -.
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   1: Evidence at protein level;
KW   3D-structure; Chaperone; Cytoplasm; Direct protein sequencing;
KW   Reference proteome; RNA-binding.
FT   CHAIN           1..232
FT                   /note="RNA chaperone ProQ"
FT                   /id="PRO_0000214614"
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"
FT   STRAND          183..186
FT                   /evidence="ECO:0007829|PDB:5NBB"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:5NBB"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:5NBB"
FT   STRAND          210..217
FT                   /evidence="ECO:0007829|PDB:5NBB"
FT   TURN            227..229
FT                   /evidence="ECO:0007829|PDB:5NBB"
SQ   SEQUENCE   232 AA;  25893 MW;  042BEAA345A3C739 CRC64;
     MENQPKLNSS KEVIAFLAER FPHCFSAEGE ARPLKIGIFQ DLVDRVAGEM NLSKTQLRSA
     LRLYTSSWRY LYGVKPGATR VDLDGNPCGE LDEQHVEHAR KQLEEAKARV QAQRAEQQAK
     KREAAATAGE KEDAPRRERK PRPTTPRRKE GAERKPRAQK PVEKAPKTVK APREEQHTPV
     SDISALTVGQ ALKVKAGQNA MDATVLEITK DGVRVQLNSG MSLIVRAEHL VF