ID A0A0S1SM96_9BACT Unreviewed; 116 AA.
AC A0A0S1SM96; A0A0S1SJP5; A0A0S1SL43; A0A0S1STX8; A0A0S1SWR1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Translational regulator CsrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN ORFNames=PeribacterD1_1123 {ECO:0000313|EMBL:ALM13783.1};
OS Candidatus Peribacter riflensis.
OC Bacteria; Candidatus Peregrinibacteria; Candidatus Peribacteria;
OC Candidatus Peribacterales; Candidatus Peribacteraceae; Peribacter.
OX NCBI_TaxID=1735162 {ECO:0000313|EMBL:ALM13783.1, ECO:0000313|Proteomes:UP000069135};
RN [1] {ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALM13783.1, ECO:0000313|Proteomes:UP000069135}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIFOXYD1_FULL_PER-ii_59_16 {ECO:0000313|EMBL:ALM13783.1};
RX PubMed=26844018;
RA Anantharaman K., Brown C.T., Burstein D., Castelle C.J., Probst A.J.,
RA Thomas B.C., Williams K.H., Banfield J.F.;
RT "Analysis of five complete genome sequences for members of the class
RT Peribacteria in the recently recognized Peregrinibacteria bacterial
RT phylum.";
RL PeerJ 4:E1607-E1607(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: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; CP013065; ALM13783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S1SM96; -.
DR STRING; 1735162.PeribacterB2_1125; -.
DR KEGG; prf:PeribacterA2_1123; -.
DR PATRIC; fig|1735161.3.peg.1098; -.
DR Proteomes; UP000069135; 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; 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 Bacterial flagellum biogenesis {ECO:0000256|HAMAP-Rule:MF_00167};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00167};
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}.
FT REGION 95..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 116 AA; 12503 MW; 940E2E6205CFCE1D CRC64;
MTVKVFLSSR QAGGSLACRE LNGPSEVGPS LFPLSASRRL EDAVLVLSRK KNESIVINDD
ITIVVVEIRG DKVRLGVEAP KEVPVHRREV FDAIRRNEAA TEEKPTGGQD GPPATG
//
