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Database: UniProt
Entry: B5JV96_9GAMM
LinkDB: B5JV96_9GAMM
Original site: B5JV96_9GAMM 
ID   B5JV96_9GAMM            Unreviewed;        64 AA.
AC   B5JV96;
DT   14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2008, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=Translational regulator CsrA {ECO:0000256|HAMAP-Rule:MF_00167};
DE   AltName: Full=Carbon storage regulator {ECO:0000256|HAMAP-Rule:MF_00167};
GN   Name=csrA {ECO:0000256|HAMAP-Rule:MF_00167,
GN   ECO:0000313|EMBL:EDY86394.1};
GN   ORFNames=GP5015_312 {ECO:0000313|EMBL:EDY86394.1};
OS   gamma proteobacterium HTCC5015.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY86394.1, ECO:0000313|Proteomes:UP000004692};
RN   [1] {ECO:0000313|Proteomes:UP000004692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX   PubMed=20472792; DOI=10.1128/JB.00510-10;
RA   Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequence of the novel marine member of the Gammaproteobacteria
RT   strain HTCC5015.";
RL   J. Bacteriol. 192:3838-3839(2010).
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:0000256|HAMAP-Rule:MF_00167}.
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:0000256|HAMAP-Rule:MF_00167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00167}.
CC   -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00167}.
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DR   EMBL; DS990603; EDY86394.1; -; Genomic_DNA.
DR   AlphaFoldDB; B5JV96; -.
DR   STRING; 391615.GP5015_312; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_2_1_6; -.
DR   OrthoDB; 9809061at2; -.
DR   Proteomes; UP000004692; Unassembled WGS sequence.
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; Translational regulator CsrA; 1.
DR   HAMAP; MF_00167; CsrA; 1.
DR   InterPro; IPR003751; CsrA.
DR   InterPro; IPR036107; CsrA_sf.
DR   NCBIfam; TIGR00202; csrA; 1.
DR   PANTHER; PTHR34984; CARBON STORAGE REGULATOR; 1.
DR   PANTHER; PTHR34984:SF1; CARBON STORAGE REGULATOR; 1.
DR   Pfam; PF02599; CsrA; 1.
DR   SUPFAM; SSF117130; CsrA-like; 1.
PE   3: Inferred from homology;
KW   Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_00167};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000004692};
KW   Repressor {ECO:0000256|HAMAP-Rule:MF_00167};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00167};
KW   Translation regulation {ECO:0000256|ARBA:ARBA00022845, ECO:0000256|HAMAP-
KW   Rule:MF_00167}.
SQ   SEQUENCE   64 AA;  7201 MW;  7A531E31DEC304D0 CRC64;
     MLILTRRVGE TLMVGDDVTV TVLGVKGNQV RIGVNAPKEI AVHREEIYER IKREQDDPDS
     IGNR
//
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