CSRA_ECOLI
ID CSRA_ECOLI Reviewed; 61 AA.
AC P69913; P31803;
DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Carbon storage regulator {ECO:0000305};
DE AltName: Full=Translational dual regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167, ECO:0000303|PubMed:8393005};
GN Synonyms=zfiA {ECO:0000303|PubMed:8604133};
GN OrderedLocusNames=b2696, JW2666;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW3414;
RX PubMed=8393005; DOI=10.1128/jb.175.15.4744-4755.1993;
RA Romeo T., Gong M., Liu M.-Y., Brun-Zinkernagel A.-M.;
RT "Identification and molecular characterization of csrA, a pleiotropic gene
RT from Escherichia coli that affects glycogen biosynthesis, gluconeogenesis,
RT cell size, and surface properties.";
RL J. Bacteriol. 175:4744-4755(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=KP4714;
RX PubMed=8604133; DOI=10.1006/jmbi.1996.0103;
RA Murayama N., Shimizu H., Takiguchi S., Baba Y., Amino H., Horiuchi T.,
RA Sekimizu K., Miki T.;
RT "Evidence for involvement of Escherichia coli genes pmbA, csrA and a
RT previously unrecognized gene tldD, in the control of DNA gyrase by letD
RT (ccdB) of sex factor F.";
RL J. Mol. Biol. 256:483-502(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
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 [5]
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 [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW3414;
RX PubMed=7751274; DOI=10.1128/jb.177.10.2663-2672.1995;
RA Liu M.Y., Yang H., Romeo T.;
RT "The product of the pleiotropic Escherichia coli gene csrA modulates
RT glycogen biosynthesis via effects on mRNA stability.";
RL J. Bacteriol. 177:2663-2672(1995).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW3414;
RX PubMed=7493933; DOI=10.1074/jbc.270.49.29096;
RA Sabnis N.A., Yang H., Romeo T.;
RT "Pleiotropic regulation of central carbohydrate metabolism in Escherichia
RT coli via the gene csrA.";
RL J. Biol. Chem. 270:29096-29104(1995).
RN [8]
RP ANTAGONIZED BY CSRB, SUBUNIT, INTERACTION WITH SRNA CSRB, RNA-BINDING, AND
RP POSSIBLE CSRA-BINDING SITE.
RX PubMed=9211896; DOI=10.1074/jbc.272.28.17502;
RA Liu M.Y., Gui G., Wei B., Preston J.F. III, Oakford L., Yuksel U.,
RA Giedroc D.P., Romeo T.;
RT "The RNA molecule CsrB binds to the global regulatory protein CsrA and
RT antagonizes its activity in Escherichia coli.";
RL J. Biol. Chem. 272:17502-17510(1997).
RN [9]
RP FUNCTION IN MOTILITY REGULATION.
RX PubMed=11298291; DOI=10.1046/j.1365-2958.2001.02380.x;
RA Wei B.L., Brun-Zinkernagel A.-M., Simecka J.W., Pruess B.M., Babitzke P.,
RA Romeo T.;
RT "Positive regulation of motility and flhDC expression by the RNA-binding
RT protein CsrA of Escherichia coli.";
RL Mol. Microbiol. 40:245-256(2001).
RN [10]
RP FUNCTION IN BIOFILM REPRESSION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=11741870; DOI=10.1128/jb.184.1.290-301.2002;
RA Jackson D.W., Suzuki K., Oakford L., Simecka J.W., Hart M.E., Romeo T.;
RT "Biofilm formation and dispersal under the influence of the global
RT regulator CsrA of Escherichia coli.";
RL J. Bacteriol. 184:290-301(2002).
RN [11]
RP FUNCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12193630; DOI=10.1128/jb.184.18.5130-5140.2002;
RA Suzuki K., Wang X., Weilbacher T., Pernestig A.-K., Melefors O.,
RA Georgellis D., Babitzke P., Romeo T.;
RT "Regulatory circuitry of the CsrA/CsrB and BarA/UvrY systems of Escherichia
RT coli.";
RL J. Bacteriol. 184:5130-5140(2002).
RN [12]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=12067347; DOI=10.1046/j.1365-2958.2002.02982.x;
RA Baker C.S., Morozov I., Suzuki K., Romeo T., Babitzke P.;
RT "CsrA regulates glycogen biosynthesis by preventing translation of glgC in
RT Escherichia coli.";
RL Mol. Microbiol. 44:1599-1610(2002).
RN [13]
RP ANTAGONIZED BY CSRB AND CSRC, SUBUNIT, INTERACTION WITH SRNA CSRC,
RP DISRUPTION PHENOTYPE, AND RNA-BINDING.
RX PubMed=12694612; DOI=10.1046/j.1365-2958.2003.03459.x;
RA Weilbacher T., Suzuki K., Dubey A.K., Wang X., Gudapaty S., Morozov I.,
RA Baker C.S., Georgellis D., Babitzke P., Romeo T.;
RT "A novel sRNA component of the carbon storage regulatory system of
RT Escherichia coli.";
RL Mol. Microbiol. 48:657-670(2003).
RN [14]
RP INDUCTION.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290, K12 / DH5-alpha, and
RC K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16352847; DOI=10.1128/jb.188.1.305-316.2006;
RA Gonzalez Barrios A.F., Zuo R., Hashimoto Y., Yang L., Bentley W.E.,
RA Wood T.K.;
RT "Autoinducer 2 controls biofilm formation in Escherichia coli through a
RT novel motility quorum-sensing regulator (MqsR, B3022).";
RL J. Bacteriol. 188:305-316(2006).
RN [15]
RP FUNCTION, DOMAIN, MUTAGENESIS OF LEU-2; ILE-3; LEU-4; ARG-6; ARG-7; THR-19;
RP ASN-35; VAL-40; VAL-42; ARG-44 AND ILE-47, AND RNA-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16923806; DOI=10.1074/jbc.m606057200;
RA Mercante J., Suzuki K., Cheng X., Babitzke P., Romeo T.;
RT "Comprehensive alanine-scanning mutagenesis of Escherichia coli CsrA
RT defines two subdomains of critical functional importance.";
RL J. Biol. Chem. 281:31832-31842(2006).
RN [16]
RP PARTIALLY SUPPRESSES AN RSGA MUTANT.
RC STRAIN=K12;
RX PubMed=18223068; DOI=10.1128/jb.01744-07;
RA Campbell T.L., Brown E.D.;
RT "Genetic interaction screens with ordered overexpression and deletion clone
RT sets implicate the Escherichia coli GTPase YjeQ in late ribosome
RT biogenesis.";
RL J. Bacteriol. 190:2537-2545(2008).
RN [17]
RP RNA-BINDING, FUNCTION IN DIGUANYLATE CYCLASE REGULATION, AND INDUCTION.
RC STRAIN=K12;
RX PubMed=18713317; DOI=10.1111/j.1365-2958.2008.06411.x;
RA Jonas K., Edwards A.N., Simm R., Romeo T., Romling U., Melefors O.;
RT "The RNA binding protein CsrA controls cyclic di-GMP metabolism by directly
RT regulating the expression of GGDEF proteins.";
RL Mol. Microbiol. 70:236-257(2008).
RN [18]
RP DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19103924; DOI=10.1128/jb.01573-08;
RA Timmermans J., Van Melderen L.;
RT "Conditional essentiality of the csrA gene in Escherichia coli.";
RL J. Bacteriol. 191:1722-1724(2009).
RN [19]
RP FUNCTION IN BIOFILM FORMATION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / AB400;
RX PubMed=19460094; DOI=10.1111/j.1365-2958.2009.06739.x;
RA Boehm A., Steiner S., Zaehringer F., Casanova A., Hamburger F., Ritz D.,
RA Keck W., Ackermann M., Schirmer T., Jenal U.;
RT "Second messenger signalling governs Escherichia coli biofilm induction
RT upon ribosomal stress.";
RL Mol. Microbiol. 72:1500-1516(2009).
RN [20]
RP FUNCTION, REGULON, DISRUPTION PHENOTYPE, AND RNA-BINDING.
RC STRAIN=K12 / CF7789, and K12 / MG1655 / ATCC 47076;
RX PubMed=21488981; DOI=10.1111/j.1365-2958.2011.07663.x;
RA Edwards A.N., Patterson-Fortin L.M., Vakulskas C.A., Mercante J.W.,
RA Potrykus K., Vinella D., Camacho M.I., Fields J.A., Thompson S.A.,
RA Georgellis D., Cashel M., Babitzke P., Romeo T.;
RT "Circuitry linking the Csr and stringent response global regulatory
RT systems.";
RL Mol. Microbiol. 80:1561-1580(2011).
RN [21]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / CF7789;
RX PubMed=21696456; DOI=10.1111/j.1365-2958.2011.07723.x;
RA Yakhnin H., Yakhnin A.V., Baker C.S., Sineva E., Berezin I., Romeo T.,
RA Babitzke P.;
RT "Complex regulation of the global regulatory gene csrA: CsrA-mediated
RT translational repression, transcription from five promoters by Esigma(70)
RT and Esigma(S), and indirect transcriptional activation by CsrA.";
RL Mol. Microbiol. 81:689-704(2011).
RN [22]
RP FUNCTION, AND RNA-BINDING.
RC STRAIN=K12 / CF7789;
RX PubMed=28851853; DOI=10.1128/mbio.01355-17;
RA Park H., McGibbon L.C., Potts A.H., Yakhnin H., Romeo T., Babitzke P.;
RT "Translational repression of the RpoS antiadapter IraD by CsrA is mediated
RT via translational coupling to a short upstream open reading frame.";
RL MBio 8:0-0(2017).
RN [23]
RP FUNCTION, DISRUPTION PHENOTYPE, AND RNA-BINDING.
RC STRAIN=K12 / CF7789;
RX PubMed=28924029; DOI=10.1128/jb.00484-17;
RA Yakhnin H., Aichele R., Ades S.E., Romeo T., Babitzke P.;
RT "Circuitry linking the global Csr and sigma(E)-dependent cell envelope
RT stress response systems.";
RL J. Bacteriol. 0:0-0(2017).
RN [24]
RP REVIEW.
RX PubMed=25833324; DOI=10.1128/mmbr.00052-14;
RA Vakulskas C.A., Potts A.H., Babitzke P., Ahmer B.M., Romeo T.;
RT "Regulation of bacterial virulence by Csr (Rsm) systems.";
RL Microbiol. Mol. Biol. Rev. 79:193-224(2015).
RN [25]
RP STRUCTURE BY NMR, RNA-BINDING, AND SUBUNIT.
RX PubMed=15866937; DOI=10.1128/jb.187.10.3496-3501.2005;
RA Gutierrez P., Li Y., Osborne M.J., Pomerantseva E., Liu Q., Gehring K.;
RT "Solution structure of the carbon storage regulator protein CsrA from
RT Escherichia coli.";
RL J. Bacteriol. 187:3496-3501(2005).
CC -!- FUNCTION: A key translational regulator that binds mRNA to regulate
CC translation initiation and/or mRNA stability, initially identified for
CC its effects on central carbon metabolism (PubMed:8393005). Mediates
CC global changes in gene expression, shifting from rapid growth to stress
CC survival by linking envelope stress, the stringent response and the
CC catabolite repression systems (PubMed:21488981, PubMed:28924029). Binds
CC to the 5'-UTR of mRNA to repress or activate translation; 2 binding
CC sites on the homodimer can bridge 2 sites within target RNA (By
CC similarity). Exerts reciprocal effects on enzymes of gluconeogenesis
CC and glycogen biosynthesis versus those of glycolysis (PubMed:7493933,
CC PubMed:16923806). Negatively effects glycogen biosynthesis,
CC gluconeogenesis, alters cell size and surface properties
CC (PubMed:8393005, PubMed:7751274, PubMed:7493933). Activates regulates
CC expression of glycolysis genes (PubMed:7493933). Represses biofilm
CC formation (PubMed:11741870). Regulates glycogen synthesis under both
CC aerobic and anaerobic conditions; overexpression strongly inhibits
CC glycogen accumulation (PubMed:8393005). Binds to 4 sites in its own
CC promoter, including the Shine-Dalgarno sequence, repressing its own
CC translation; mutating the binding-sites decreases repression
CC (PubMed:21696456). Indirectly activates transcription from 1 of its 5
CC promoters, which is responsible for increased expression during
CC stationary phase (PubMed:21696456). Binds to at least 720 transcripts
CC in strain K12 / CF7789, many of which are also part of the stringent
CC response, including relA, spoT and dksA; slightly represses RelA and
CC slightly activates DskA translation (PubMed:21488981). Binds to and
CC represses the ECF sigma factor rpoE promoter (PubMed:28924029).
CC Accelerates the degradation of glgC gene transcripts; overexpression
CC further decreases glgC transcripts (PubMed:7751274). Binds 2 sites in
CC the glgC mRNA leader, 1 of which overlaps the Shine-Dalgarno sequence,
CC preventing ribosome-binding and thus destabilizing the mRNA
CC (PubMed:12067347). Acts to inhibit interaction between the CcdB (also
CC known as LetD) protein and the A subunit of DNA gyrase
CC (PubMed:8604133). Required to activate motility and flagellum
CC biosynthesis through the post-transcriptional activation of flhDC
CC expression by binding to and stabilizing the flhDC message
CC (PubMed:11298291). Represses translation of iraD mRNA via translational
CC coupling to an upstream open reading frame (PubMed:28851853). Binds to
CC mRNA and reduces levels of probable diguanylate cyclases dgcT and dgcZ
CC (PubMed:18713317). {ECO:0000250|UniProtKB:P0DPC3,
CC ECO:0000269|PubMed:11298291, ECO:0000269|PubMed:11741870,
CC ECO:0000269|PubMed:12067347, ECO:0000269|PubMed:16923806,
CC ECO:0000269|PubMed:18713317, ECO:0000269|PubMed:19460094,
CC ECO:0000269|PubMed:21488981, ECO:0000269|PubMed:21696456,
CC ECO:0000269|PubMed:28851853, ECO:0000269|PubMed:28924029,
CC ECO:0000269|PubMed:7493933, ECO:0000269|PubMed:7751274,
CC ECO:0000269|PubMed:8393005, ECO:0000269|PubMed:8604133}.
CC -!- FUNCTION: Binds to and is sequestered by non-coding small RNAs (sRNA)
CC CsrB and CsrC which antagonize the activity of CsrA (PubMed:9211896,
CC PubMed:12694612). The consensus RNA-binding site is CAGGA(U/A/C)G which
CC is located in probable hairpin loops (PubMed:9211896). There are 18
CC sites in CsrB, which cooperatively binds about 18 copies of CsrA
CC (PubMed:9211896, PubMed:12694612). CsrC has 9 sites, and cooperatively
CC binds multiple copies of CsrA (PubMed:12694612). Indirectly activates
CC expression of CsrB and CsrC, both dependently and independently of the
CC BarA-UvrY two-component system (PubMed:12193630, PubMed:12694612).
CC ppGpp activates transcription of CsrA-antagonistic small RNAs CsrB and
CC CsrC, which down-regulates CsrA's action on translation during the
CC stringent response (PubMed:21488981). {ECO:0000269|PubMed:12193630,
CC ECO:0000269|PubMed:12694612, ECO:0000269|PubMed:9211896}.
CC -!- SUBUNIT: Homodimer; the beta-strands of each monomer intercalate to
CC form a hydrophobic core while the alpha-helices form wings that extend
CC away from the core (PubMed:15866937, ECO:0000255|HAMAP-Rule:MF_00167).
CC {ECO:0000269|PubMed:15866937}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- INDUCTION: Activated by MqsR (PubMed:16352847, PubMed:18713317).
CC Activated by DksA and (p)ppGpp, under partial control of RpoS, the
CC sigma stress factor (at protein level) (PubMed:21488981). Binds to 4
CC sites in its own mRNA and represses translation (PubMed:21696456).
CC Expressed from 5 promoters; P2 and P5 depend on housekeeping sigma
CC factor 70 (rpoD) while P1 and P3 2 depend on RpoS; indirect activation
CC of P3 leads to increased transcription during the log to stationary
CC phase shift (PubMed:21696456). {ECO:0000269|PubMed:16352847,
CC ECO:0000269|PubMed:18713317, ECO:0000269|PubMed:21488981,
CC ECO:0000269|PubMed:21696456}.
CC -!- DOMAIN: Two regions important for regulation and RNA-binding are found
CC in the N-terminus (residues 2-7) and middle (residues 40-47). Both are
CC part of the intercalated beta-strands that form the hydrophobic core of
CC the protein; region 1 from one monomer contacts region 2 of the other.
CC The homodimer has 2 distinct RNA-binding regions on opposite, solvent-
CC exposed surface of the protein. {ECO:0000269|PubMed:16923806}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be deleted when cells grow
CC on LB but cells will grow with pyruvate as the sole carbon source; if
CC glycogen synthesis is impaired then cells become viable
CC (PubMed:19103924). Most deletion experiments use an allele which has a
CC kanamycin-resistance cassette inserted after amino acid 50, which
CC retains about 10% residual activity (PubMed:8393005, PubMed:19103924).
CC Increased levels of glgC transcripts during both exponential and
CC stationary phases (PubMed:7751274). Decreased levels of enzymes
CC involved in glycolysis (PubMed:7493933). Increased biofilm formation
CC (PubMed:11741870). Decreased expression of it antagonistic small RNAs
CC CsrB and CsrC (PubMed:12694612). Allows basal levels of poly-GlcNAc
CC synthesis and biofilm formation; this disrupted strain serves as a
CC model system for biofilm formation (PubMed:19460094). Increased
CC expression of RelA, about 1.5-fold increase in (p)ppGpp levels
CC (PubMed:21488981). Increased levels of ECF sigma factor E (rpoE)
CC (PubMed:28924029). {ECO:0000269|PubMed:11741870,
CC ECO:0000269|PubMed:12694612, ECO:0000269|PubMed:19103924,
CC ECO:0000269|PubMed:19460094, ECO:0000269|PubMed:21488981,
CC ECO:0000269|PubMed:28924029, ECO:0000269|PubMed:7493933,
CC ECO:0000269|PubMed:7751274, ECO:0000269|PubMed:8393005}.
CC -!- MISCELLANEOUS: Identified as a multicopy suppressor of the slow growth
CC phenotype of an rsgA (yjeQ) deletion mutant.
CC {ECO:0000269|PubMed:18223068}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC Rule:MF_00167}.
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DR EMBL; L07596; AAA71919.1; -; Unassigned_DNA.
DR EMBL; D44453; BAA21555.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75738.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16558.1; -; Genomic_DNA.
DR PIR; B40608; B40608.
DR RefSeq; NP_417176.1; NC_000913.3.
DR RefSeq; WP_000906486.1; NZ_STEB01000027.1.
DR PDB; 1Y00; NMR; -; A/B=1-61.
DR PDB; 5Z38; X-ray; 2.29 A; E/G/I/K=1-44, F/H/J/L=1-61.
DR PDBsum; 1Y00; -.
DR PDBsum; 5Z38; -.
DR AlphaFoldDB; P69913; -.
DR SMR; P69913; -.
DR BioGRID; 4259421; 231.
DR BioGRID; 851508; 4.
DR DIP; DIP-47836N; -.
DR IntAct; P69913; 10.
DR STRING; 511145.b2696; -.
DR jPOST; P69913; -.
DR PaxDb; P69913; -.
DR PRIDE; P69913; -.
DR EnsemblBacteria; AAC75738; AAC75738; b2696.
DR EnsemblBacteria; BAA16558; BAA16558; BAA16558.
DR GeneID; 64727209; -.
DR GeneID; 67517504; -.
DR GeneID; 947176; -.
DR KEGG; ecj:JW2666; -.
DR KEGG; eco:b2696; -.
DR PATRIC; fig|1411691.4.peg.4048; -.
DR EchoBASE; EB1416; -.
DR eggNOG; COG1551; Bacteria.
DR HOGENOM; CLU_164837_2_1_6; -.
DR InParanoid; P69913; -.
DR OMA; IHRKEVY; -.
DR PhylomeDB; P69913; -.
DR BioCyc; EcoCyc:EG11447-MON; -.
DR EvolutionaryTrace; P69913; -.
DR PRO; PR:P69913; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IDA:EcoCyc.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0048255; P:mRNA stabilization; IMP:CACAO.
DR GO; GO:0045719; P:negative regulation of glycogen biosynthetic process; IDA:EcoCyc.
DR GO; GO:0031438; P:negative regulation of mRNA cleavage; IDA:CACAO.
DR GO; GO:0017148; P:negative regulation of translation; IMP:CACAO.
DR GO; GO:0045947; P:negative regulation of translational initiation; IDA:EcoCyc.
DR GO; GO:0045948; P:positive regulation of translational initiation; IDA:EcoCyc.
DR Gene3D; 2.60.40.4380; -; 1.
DR HAMAP; MF_00167; CsrA; 1.
DR InterPro; IPR003751; CsrA.
DR InterPro; IPR036107; CsrA_sf.
DR PANTHER; PTHR34984; PTHR34984; 1.
DR Pfam; PF02599; CsrA; 1.
DR SUPFAM; SSF117130; SSF117130; 1.
DR TIGRFAMs; TIGR00202; csrA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Cytoplasm; Reference proteome; Repressor;
KW RNA-binding; Translation regulation.
FT CHAIN 1..61
FT /note="Carbon storage regulator"
FT /id="PRO_0000177061"
FT REGION 2..7
FT /note="Region 1, important for regulation and mRNA-binding"
FT /evidence="ECO:0000269|PubMed:16923806"
FT REGION 40..47
FT /note="Region 2, important for regulation and mRNA-binding"
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 2
FT /note="L->A: Loss of in vivo repression and activation, 73-
FT fold decreased affinity for RNA, about 75% wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 3
FT /note="I->A: 80% loss of in vivo repression and activation,
FT about 20% wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 4
FT /note="L->A: 90% loss of in vivo repression and activation,
FT 60-fold decreased affinity for RNA, about 60% wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 6
FT /note="R->A: Nearly complete loss of in vivo repression and
FT activation, 30-fold decreased affinity for RNA, about 175%
FT wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 7
FT /note="R->A: 70% loss of in vivo repression and activation,
FT 12-fold decreased affinity for RNA, about 125% wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 19
FT /note="T->A: Increased repression and activation in vivo,
FT about 75% wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 35
FT /note="N->A: Increased repression and activation in vivo,
FT about 75% wild-type protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 40
FT /note="V->A: 90% loss of in vivo repression and activation,
FT 67-fold decreased affinity for RNA, about 75% wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 42
FT /note="V->A: Loss of in vivo repression and activation,
FT 135-fold decreased affinity for RNA, about 40% wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 44
FT /note="R->A: Loss of in vivo repression and activation,
FT 150-fold decreased affinity for RNA, >500% wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT MUTAGEN 47
FT /note="I->A: 90% loss of in vivo repression and activation,
FT 67-fold decreased affinity for RNA, about 150% wild-type
FT protein levels."
FT /evidence="ECO:0000269|PubMed:16923806"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5Z38"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:5Z38"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:5Z38"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:5Z38"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:5Z38"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:5Z38"
FT HELIX 45..53
FT /evidence="ECO:0007829|PDB:5Z38"
SQ SEQUENCE 61 AA; 6856 MW; 16308FC572670E1C CRC64;
MLILTRRVGE TLMIGDEVTV TVLGVKGNQV RIGVNAPKEV SVHREEIYQR IQAEKSQQSS
Y
