ID   CSRA_PECPM              Reviewed;          61 AA.
AC   K4FF95; Q47620; Q9XB50;
DT   06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2013, sequence version 1.
DT   25-MAY-2022, entry version 54.
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 RsmA;
GN   Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; Synonyms=rsmA;
GN   OrderedLocusNames=W5S_1009;
OS   Pectobacterium parmentieri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=1905730;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SCC3193;
RA   Andersson R.A.;
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCC3193;
RX   PubMed=23045508; DOI=10.1128/jb.00681-12;
RA   Koskinen J.P., Laine P., Niemi O., Nykyri J., Harjunpaa H., Auvinen P.,
RA   Paulin L., Pirhonen M., Palva T., Holm L.;
RT   "Genome sequence of Pectobacterium sp. strain SCC3193.";
RL   J. Bacteriol. 194:6004-6004(2012).
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: Controls extracellular enzymes, N-(3-oxohexanoyl)-L-
CC       homoserine lactone, and pathogenicity. Repressor of virulence factors
CC       (By similarity). {ECO:0000250|UniProtKB:P0DKY7}.
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; AJ238885; CAB46440.1; -; Genomic_DNA.
DR   EMBL; CP003415; AFI89127.1; -; Genomic_DNA.
DR   RefSeq; WP_005972168.1; NZ_QESW01000022.1.
DR   AlphaFoldDB; K4FF95; -.
DR   SMR; K4FF95; -.
DR   STRING; 1905730.W5S_1009; -.
DR   EnsemblBacteria; AFI89127; AFI89127; W5S_1009.
DR   GeneID; 51390816; -.
DR   GeneID; 9734939; -.
DR   KEGG; pec:W5S_1009; -.
DR   PATRIC; fig|1166016.3.peg.1022; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_2_1_6; -.
DR   OMA; IHRKEVY; -.
DR   OrthoDB; 2032250at2; -.
DR   Proteomes; UP000008044; Chromosome.
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..61
FT                   /note="Translational regulator CsrA"
FT                   /id="PRO_0000421829"
SQ   SEQUENCE   61 AA;  6839 MW;  16308BD4C2670E1C CRC64;
     MLILTRRVGE TLMIGDEVTV TVLGVKGNQV RIGVNAPKEV SVHREEIYQR IQAEKSQPTS
     Y