CSRA_GEOTN
ID CSRA_GEOTN Reviewed; 82 AA.
AC A4ISU9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Translational regulator CsrA {ECO:0000255|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000255|HAMAP-Rule:MF_00167}; OrderedLocusNames=GTNG_3058;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
RN [2] {ECO:0007744|PDB:5DMB}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 2-82 IN COMPLEX WITH FLIW,
RP SUBUNIT, AND DOMAIN.
RC STRAIN=NG-80;
RX PubMed=27551070; DOI=10.1073/pnas.1602425113;
RA Altegoer F., Rensing S.A., Bange G.;
RT "Structural basis for the CsrA-dependent modulation of translation
RT initiation by an ancient regulatory protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:10168-10173(2016).
CC -!- FUNCTION: A translational regulator that binds mRNA to regulate
CC translation initiation and/or mRNA stability. Usually binds in the 5'-
CC UTR at or near the Shine-Dalgarno sequence preventing ribosome-binding,
CC thus repressing translation. Its main target seems to be the major
CC flagellin gene, while its function is anatagonized by FliW.
CC {ECO:0000255|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. Each of the alpha-helical wings interacts with an
CC FliW monomer, yielding a FliW-CsrA(2)-FliW complex.
CC {ECO:0000269|PubMed:27551070}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00167}.
CC -!- DOMAIN: Interacts with FliW via its C-terminal alpha helices
CC (approximately 44-57 and 63-74).
CC -!- SIMILARITY: Belongs to the CsrA/RsmA family. {ECO:0000255|HAMAP-
CC Rule:MF_00167}.
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DR EMBL; CP000557; ABO68403.1; -; Genomic_DNA.
DR RefSeq; WP_011888204.1; NC_009328.1.
DR PDB; 5DMB; X-ray; 2.30 A; D=2-82.
DR PDBsum; 5DMB; -.
DR AlphaFoldDB; A4ISU9; -.
DR SMR; A4ISU9; -.
DR STRING; 420246.GTNG_3058; -.
DR EnsemblBacteria; ABO68403; ABO68403; GTNG_3058.
DR KEGG; gtn:GTNG_3058; -.
DR eggNOG; COG1551; Bacteria.
DR HOGENOM; CLU_164837_0_2_9; -.
DR OMA; IHRKEVY; -.
DR OrthoDB; 2032250at2; -.
DR Proteomes; UP000001578; 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:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
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:1902208; P:regulation of bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006109; P:regulation of carbohydrate metabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum biogenesis; Cytoplasm; Repressor;
KW RNA-binding; Translation regulation.
FT CHAIN 1..82
FT /note="Translational regulator CsrA"
FT /id="PRO_1000023385"
FT STRAND 11..14
FT /evidence="ECO:0007829|PDB:5DMB"
FT TURN 15..17
FT /evidence="ECO:0007829|PDB:5DMB"
FT STRAND 18..25
FT /evidence="ECO:0007829|PDB:5DMB"
FT STRAND 27..35
FT /evidence="ECO:0007829|PDB:5DMB"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:5DMB"
FT HELIX 63..72
FT /evidence="ECO:0007829|PDB:5DMB"
SQ SEQUENCE 82 AA; 9076 MW; 181FB8D890C95E10 CRC64;
MLVLTRKLKE AIQIGDDIEI TVLAIQGDQV KLGINAPKHV EIHRKEIYLA IQAENNAASH
ASKSSLKRLN EQLKHLKGGK QA