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Database: UniProt
Entry: W0E2H9_MARPU
LinkDB: W0E2H9_MARPU
Original site: W0E2H9_MARPU 
ID   W0E2H9_MARPU            Unreviewed;        72 AA.
AC   W0E2H9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
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   ORFNames=MARPU_14725 {ECO:0000313|EMBL:AHF04957.1};
OS   Marichromatium purpuratum 984.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Marichromatium.
OX   NCBI_TaxID=765910 {ECO:0000313|EMBL:AHF04957.1, ECO:0000313|Proteomes:UP000005275};
RN   [1] {ECO:0000313|EMBL:AHF04957.1, ECO:0000313|Proteomes:UP000005275}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=984 {ECO:0000313|EMBL:AHF04957.1,
RC   ECO:0000313|Proteomes:UP000005275};
RG   DOE Joint Genome Institute;
RA   Bryant D.A., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
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; CP007031; AHF04957.1; -; Genomic_DNA.
DR   RefSeq; WP_005224038.1; NZ_CP007031.1.
DR   AlphaFoldDB; W0E2H9; -.
DR   STRING; 765910.MARPU_14725; -.
DR   KEGG; mpur:MARPU_14725; -.
DR   eggNOG; COG1551; Bacteria.
DR   HOGENOM; CLU_164837_2_1_6; -.
DR   OrthoDB; 9809061at2; -.
DR   Proteomes; UP000005275; 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; 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:UP000005275};
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   72 AA;  7898 MW;  00E254050E1B59C9 CRC64;
     MLILTRRVGE TLMVGDEVTV TVLGVKGNQV RIGVNAPRDV AVHREEIYER IKREQAETTP
     GVAVVDQGGQ IE
//
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