CSRA_PSEAE
ID CSRA_PSEAE Reviewed; 61 AA.
AC O69078;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
DE AltName: Full=Carbon storage regulator {ECO:0000255|HAMAP-Rule:MF_00167};
DE AltName: Full=Global translational regulatory protein RsmA {ECO:0000303|PubMed:11673439};
GN Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN Synonyms=rsmA {ECO:0000303|PubMed:11673439}; OrderedLocusNames=PA0905;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN TRANSLATION REPRESSION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11673439; DOI=10.1128/jb.183.22.6676-6683.2001;
RA Pessi G., Williams F., Hindle Z., Heurlier K., Holden M.T., Camara M.,
RA Haas D., Williams P.;
RT "The global posttranscriptional regulator RsmA modulates production of
RT virulence determinants and N-acylhomoserine lactones in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 183:6676-6683(2001).
RN [2]
RP ERRATUM OF PUBMED:11673439.
RA Pessi G., Williams F., Hindle Z., Heurlier K., Holden M.T., Camara M.,
RA Haas D., Williams P.;
RT "The global posttranscriptional regulator RsmA modulates production of
RT virulence determinants and N-acylhomoserine lactones in Pseudomonas
RT aeruginosa.";
RL (er) J. Bacteriol. 184:335(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [4]
RP FUNCTION IN TRANSLATION ACTIVATION, SUBUNIT, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=15126453; DOI=10.1128/jb.186.10.2936-2945.2004;
RA Heurlier K., Williams F., Heeb S., Dormond C., Pessi G., Singer D.,
RA Camara M., Williams P., Haas D.;
RT "Positive control of swarming, rhamnolipid synthesis, and lipase production
RT by the posttranscriptional RsmA/RsmZ system in Pseudomonas aeruginosa
RT PAO1.";
RL J. Bacteriol. 186:2936-2945(2004).
RN [5]
RP FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF GLU-10 AND ARG-44, AND
RP RNA-BINDING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16359708; DOI=10.1016/j.jmb.2005.11.045;
RA Heeb S., Kuehne S.A., Bycroft M., Crivii S., Allen M.D., Haas D.,
RA Camara M., Williams P.;
RT "Functional analysis of the post-transcriptional regulator RsmA reveals a
RT novel RNA-binding site.";
RL J. Mol. Biol. 355:1026-1036(2006).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=16104018; DOI=10.1002/prot.20502;
RA Rife C., Schwarzenbacher R., McMullan D., Abdubek P., Ambing E.,
RA Axelrod H., Biorac T., Canaves J.M., Chiu H.-J., Deacon A.M., DiDonato M.,
RA Elsliger M.-A., Godzik A., Grittini C., Grzechnik S.K., Hale J.,
RA Hampton E., Han G.W., Haugen J., Hornsby M., Jaroszewski L., Klock H.E.,
RA Koesema E., Kreusch A., Kuhn P., Lesley S.A., Miller M.D., Moy K.,
RA Nigoghossian E., Paulsen J., Quijano K., Reyes R., Sims E., Spraggon G.,
RA Stevens R.C., van den Bedem H., Velasquez J., Vincent J., White A.,
RA Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A.;
RT "Crystal structure of the global regulatory protein CsrA from Pseudomonas
RT putida at 2.05 A resolution reveals a new fold.";
RL Proteins 61:449-453(2005).
CC -!- FUNCTION: A key translational regulator that binds mRNA to regulate
CC translation initiation and/or mRNA stability. Mediates global changes
CC in gene expression, shifting from rapid growth to stress survival by
CC linking envelope stress, the stringent response and the catabolite
CC repression systems. Usually binds in the 5'-UTR; binding at or near the
CC Shine-Dalgarno sequence prevents ribosome-binding, repressing
CC translation, binding elsewhere in the 5'-UTR can activate translation
CC and/or stabilize the mRNA. Its function is antagonized by small RNA(s).
CC {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- FUNCTION: Binds to mRNA to regulate gene activity at a post-
CC transcriptional level (Probable). Represses expression of many toxic
CC extracellular enzymes and compounds; decreases translation of lasI and
CC rhlI (PubMed:11673439). Positively controls swarming motility and
CC rhanolipid and lipase, possibly via expression of rhlA; activates
CC transcription of the CsrA/RsmA antagonistic sRNA RsmZ
CC (PubMed:15126453). Overexpression dramatically reduces extracellular
CC protease, elastase (lasB) and staphyolytic (lasA) activities, decreases
CC HCN production, decreases levels of autoinducers 3-oxo-C12-HSL (3-oxo-
CC N-(tetrahydro-2-oxo-3-furanyl)-dodecanamide) and C4-HSL (N-
CC butanoylhomoserine lactone), and abolishes production of cytotoxic
CC internal lectin PA-IL (lecA) (PubMed:11673439). Control of hcn
CC expression is post-transcriptional (PubMed:11673439). Replaces
CC endogenous gene(s) in E.coli and P.fluorescens (PubMed:16359708).
CC {ECO:0000269|PubMed:11673439, ECO:0000269|PubMed:15126453,
CC ECO:0000269|PubMed:16359708}.
CC -!- FUNCTION: Probably binds to and is sequestered by non-coding small RNA
CC (sRNA) RsmZ; overexpression of rsmZ produces very similar phenotypes to
CC deletion of rsmA, while rsmZ deletion has no phenotype
CC (PubMed:15126453). {ECO:0000269|PubMed:15126453}.
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:16104018). {ECO:0000255|HAMAP-Rule:MF_00167,
CC ECO:0000269|PubMed:16104018}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- INDUCTION: Low levels of expression in early log phase, increases about
CC 3-fold by stationary phase (at protein level) (PubMed:11673439).
CC {ECO:0000269|PubMed:11673439}.
CC -!- DISRUPTION PHENOTYPE: Grows slightly more slowly; 30% reduction in
CC staphylolytic activity, increased production of lectin PA-IL, blue-
CC green pigment pyocyanine and HCN (PubMed:11673439). Increases levels of
CC autoinducers 3-oxo-C12-HSL (3-oxo-N-(tetrahydro-2-oxo-3-furanyl)-
CC dodecanamide) and C4-HSL (N-butanoylhomoserine lactone) in early log
CC phase which becomes nearly wild-type (3-oxo-C12-HSL) or 2-fold greater
CC (C4-HSL) by late log phase (PubMed:11673439). Loss of swarming mobility
CC and rhamnolipid production, loss of sRNA RsmZ expression, decreased
CC lipase, increases synthesis of pyocyanine and HCN (PubMed:15126453).
CC Loss of swarming mobility, overproduction of pyocyanine, reduction in
CC lipase biosynthesis (PubMed:16359708). {ECO:0000269|PubMed:11673439,
CC ECO:0000269|PubMed:15126453, ECO:0000269|PubMed:16359708}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC Rule:MF_00167}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF061757; AAC16242.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04294.1; -; Genomic_DNA.
DR PIR; D83531; D83531.
DR RefSeq; NP_249596.1; NC_002516.2.
DR RefSeq; WP_003085981.1; NZ_QZGE01000007.1.
DR PDB; 1VPZ; X-ray; 2.05 A; A/B=1-61.
DR PDBsum; 1VPZ; -.
DR AlphaFoldDB; O69078; -.
DR SMR; O69078; -.
DR STRING; 287.DR97_1038; -.
DR PaxDb; O69078; -.
DR PRIDE; O69078; -.
DR DNASU; 878352; -.
DR EnsemblBacteria; AAG04294; AAG04294; PA0905.
DR GeneID; 61675155; -.
DR GeneID; 878352; -.
DR KEGG; pae:PA0905; -.
DR PATRIC; fig|208964.12.peg.940; -.
DR PseudoCAP; PA0905; -.
DR HOGENOM; CLU_164837_2_1_6; -.
DR InParanoid; O69078; -.
DR OMA; IHRKEVY; -.
DR PhylomeDB; O69078; -.
DR BioCyc; PAER208964:G1FZ6-921-MON; -.
DR EvolutionaryTrace; O69078; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0045947; P:negative regulation of translational initiation; IBA:GO_Central.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0030254; P:protein secretion by the type III secretion system; IMP:PseudoCAP.
DR GO; GO:0033103; P:protein secretion by the type VI secretion system; IMP:PseudoCAP.
DR GO; GO:0009372; P:quorum sensing; IMP:PseudoCAP.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043455; P:regulation of secondary metabolic process; IMP:PseudoCAP.
DR GO; GO:1900190; P:regulation of single-species biofilm formation; IMP:PseudoCAP.
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="Translational regulator CsrA"
FT /id="PRO_0000177080"
FT MUTAGEN 10
FT /note="E->A: Behaves like wild-type in swarming, pyocyanine
FT production and lipase biosynthesis assays."
FT /evidence="ECO:0000269|PubMed:16359708"
FT MUTAGEN 44
FT /note="R->A: Does not complement deletion in swarming,
FT pyocyanine production or lipase biosynthesis assays."
FT /evidence="ECO:0000269|PubMed:16359708"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:1VPZ"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:1VPZ"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:1VPZ"
FT STRAND 18..26
FT /evidence="ECO:0007829|PDB:1VPZ"
FT STRAND 29..37
FT /evidence="ECO:0007829|PDB:1VPZ"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1VPZ"
FT HELIX 45..54
FT /evidence="ECO:0007829|PDB:1VPZ"
SQ SEQUENCE 61 AA; 6909 MW; 3F5EDCD8AD28BB10 CRC64;
MLILTRRVGE TLMVGDDVTV TVLGVKGNQV RIGVNAPKEV AVHREEIYQR IQKEKDQEPN
H
