CSRA_PROMI
ID CSRA_PROMI Reviewed; 62 AA.
AC Q93MI1;
DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 71.
DE RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
DE AltName: Full=Carbon storage regulator {ECO:0000255|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN Synonyms=rsmA {ECO:0000303|PubMed:12488561};
OS Proteus mirabilis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=P19;
RX PubMed=12488561; DOI=10.1099/jmm.0.05024-0;
RA Liaw S.J., Lai H.C., Ho S.W., Luh K.T., Wang W.B.;
RT "Role of RsmA in the regulation of swarming motility and virulence factor
RT expression in Proteus mirabilis.";
RL J. Med. Microbiol. 52:19-28(2003).
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: Expression from a low-copy number plasmid has no effect on
CC swimming, but blocks swarming and virulence factor expression as
CC measured by cell lengthening and hemolysin, protease, urease and
CC flagellin production (PubMed:12488561). Expression destabilizes
CC hemolysin mRNA (PubMed:12488561). Complements an E.coli disruption
CC mutant (PubMed:12488561). {ECO:0000269|PubMed:12488561}.
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. {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC Rule:MF_00167}.
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DR EMBL; AF403736; AAK94932.1; -; Genomic_DNA.
DR RefSeq; WP_004244778.1; NZ_WURR01000003.1.
DR AlphaFoldDB; Q93MI1; -.
DR SMR; Q93MI1; -.
DR STRING; 584.AOUC001_13975; -.
DR GeneID; 6801540; -.
DR OMA; IHRKEVY; -.
DR OrthoDB; 2032250at2; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0048027; F:mRNA 5'-UTR binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006402; P:mRNA catabolic process; IEA:InterPro.
DR GO; GO:0045947; P:negative regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0045948; P:positive regulation of translational initiation; IEA:UniProtKB-UniRule.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
KW Activator; Cytoplasm; Repressor; RNA-binding; Translation regulation.
FT CHAIN 1..62
FT /note="Translational regulator CsrA"
FT /id="PRO_0000177079"
SQ SEQUENCE 62 AA; 6981 MW; 77093F9BD4C3325B CRC64;
MLILTRRVGE TLMIGDDVTV TVLGVKGNQV RIGVNAPKEV SVHREEIYQR IQAEKTQPTD
NY
