CSRA_SERMA
ID CSRA_SERMA Reviewed; 69 AA.
AC O85735;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=Repressor of secondary metabolites {ECO:0000303|PubMed:11287746};
GN Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN Synonyms=rsmA {ECO:0000303|PubMed:11287746};
OS Serratia marcescens.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=615;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=CH1, and SS-1;
RX PubMed=11287746; DOI=10.1159/000054028;
RA Ang S., Horng Y.-T., Shu J.-C., Soo P.-C., Liu J.-H., Yi W.-C., Lai H.-C.,
RA Luh K.-T., Ho S.-W., Swift S.;
RT "The role of RsmA in the regulation of swarming motility in Serratia
RT marcescens.";
RL J. Biomed. Sci. 8:160-169(2001).
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: Involved in the process of swarming and quorum-sensing signal
CC production; overexpression strongly inhibits swarming motility, pigment
CC and N-acylhomoserine lactone (quorum-sensing signal) production but not
CC swimming motility or swarmer cell differentiation (PubMed:11287746).
CC {ECO:0000269|PubMed:11287746}.
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 -!- INDUCTION: Transcription peaks early in exponential phase, is greater
CC at 37 than 30 degrees Celsius (PubMed:11287746).
CC {ECO:0000269|PubMed:11287746}.
CC -!- DISRUPTION PHENOTYPE: Swarming motility inititates later than in wild-
CC type; once inititated the swarming velocity is normal
CC (PubMed:11287746). {ECO:0000269|PubMed:11287746}.
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC Rule:MF_00167}.
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DR EMBL; AF074437; AAC25783.1; -; Genomic_DNA.
DR EMBL; AJ243121; CAB45388.1; -; Genomic_DNA.
DR AlphaFoldDB; O85735; -.
DR SMR; O85735; -.
DR STRING; 273526.SMDB11_0161; -.
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 2: Evidence at transcript level;
KW Activator; Cytoplasm; Repressor; RNA-binding; Translation regulation.
FT CHAIN 1..69
FT /note="Translational regulator CsrA"
FT /id="PRO_0000177089"
SQ SEQUENCE 69 AA; 7696 MW; 2256A78C31BD3F50 CRC64;
MLILTRRVGE TLMIGDEVTV TVLGVKGNQV RIGVNAPKEV SVHREEIYQR IQAEKSADDL
LIPKQRLVA