ID W4VQL1_9BACI Unreviewed; 77 AA.
AC W4VQL1;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Translational regulator CsrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN Name=csrA {ECO:0000256|HAMAP-Rule:MF_00167};
GN ORFNames=JCM21714_4267 {ECO:0000313|EMBL:GAE95059.1};
OS Gracilibacillus boraciitolerans JCM 21714.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=1298598 {ECO:0000313|EMBL:GAE95059.1, ECO:0000313|Proteomes:UP000019102};
RN [1] {ECO:0000313|EMBL:GAE95059.1, ECO:0000313|Proteomes:UP000019102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 21714 {ECO:0000313|EMBL:GAE95059.1,
RC ECO:0000313|Proteomes:UP000019102};
RA Ahmed I., Oshima K., Suda W., Kitamura K., Iida T., Ohmori Y., Fujiwara T.,
RA Hattori M., Ohkuma M.;
RT "Draft Genome Sequence of the Boron-Tolerant and Moderately Halotolerant
RT Bacterium Gracilibacillus boraciitolerans JCM 21714T.";
RL Genome Announc. 2:e00097-14(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAE95059.1}.
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DR EMBL; BAVS01000038; GAE95059.1; -; Genomic_DNA.
DR RefSeq; WP_035725774.1; NZ_BAVS01000038.1.
DR AlphaFoldDB; W4VQL1; -.
DR STRING; 1298598.JCM21714_4267; -.
DR eggNOG; COG1551; Bacteria.
DR OrthoDB; 9809061at2; -.
DR Proteomes; UP000019102; 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: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 Reference proteome {ECO:0000313|Proteomes:UP000019102};
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 77 AA; 8678 MW; 155749420E685630 CRC64;
MLVLTRKLNE AIKIGDNIEV KVIAVDGDQV KLGIDAPPQS IEVHRKEIYE AIQQENNEAA
NISTNLFDLI KKSDKKY
//
