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PROQ_ECO8A
ID   PROQ_ECO8A              Reviewed;         217 AA.
AC   B7M2A7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=RNA chaperone ProQ {ECO:0000255|HAMAP-Rule:MF_00749};
GN   Name=proQ {ECO:0000255|HAMAP-Rule:MF_00749}; OrderedLocusNames=ECIAI1_1902;
OS   Escherichia coli O8 (strain IAI1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585034;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAI1;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAQ98756.1; -; Genomic_DNA.
DR   RefSeq; WP_000431385.1; NC_011741.1.
DR   AlphaFoldDB; B7M2A7; -.
DR   SMR; B7M2A7; -.
DR   KEGG; ecr:ECIAI1_1902; -.
DR   HOGENOM; CLU_113254_0_0_6; -.
DR   OMA; WRYLKGV; -.
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..217
FT                   /note="RNA chaperone ProQ"
FT                   /id="PRO_1000133292"
FT   REGION          105..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..162
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   217 AA;  24339 MW;  3814EA0A4DFEF8CD CRC64;
     MENQPKLNSS KEVIAFLAER FPHCFSAEGE ARPLKIGIFQ DLVDRVAGEM NLSKTQLRSA
     LRLYTSSWRY LYGVKPGATR VDLDGNPCGE LDEQHVEHAR KQLEEAKARV QAQRAEQQAK
     KRERKPRPTT PRRKEGAERK PRAQKPVEKA PKTVKAPREE QHTPVSDISA LTVGQALKVK
     AGQNAMDATV LEITKDGVRV QLNSGMSLIV RAEHLVF
 
 
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