FLIW_GEOTN
ID FLIW_GEOTN Reviewed; 144 AA.
AC A4ISV0;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
DE RecName: Full=Flagellar assembly factor FliW {ECO:0000255|HAMAP-Rule:MF_01185};
GN Name=fliW {ECO:0000255|HAMAP-Rule:MF_01185}; OrderedLocusNames=GTNG_3059;
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, ECO:0007744|PDB:5DMD, ECO:0007744|PDB:5JAK}
RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 2-144 ALONE AND IN COMPLEX WITH
RP CSRA, FUNCTION, SUBUNIT, AND MUTAGENESIS OF PHE-44; GLN-123 AND ILE-125.
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: Acts as an anti-CsrA protein, binds CsrA and prevents it from
CC repressing translation of its target genes, one of which is flagellin.
CC Binds to flagellin and participates in the assembly of the flagellum.
CC {ECO:0000255|HAMAP-Rule:MF_01185}.
CC -!- FUNCTION: Allosterically inhibits CsrA binding to mRNA in a non-
CC competitive fashion by preventing CsrA binding to the 5'-UTR
CC (PubMed:27551070). {ECO:0000269|PubMed:27551070}.
CC -!- SUBUNIT: Monomer (PubMed:27551070). One copy interacts with the each
CC alpha-helical wing of the CsrA homodimer, yielding a FliW-CsrA(2)-FliW
CC complex (PubMed:27551070). Comparison with a CsrA-mRNA structure (2JPP)
CC suggests CsrA cannot bind both mRNA and FliW at the same time
CC (PubMed:27551070). Interacts with flagellin (By similarity).
CC {ECO:0000250|UniProtKB:P96503, ECO:0000269|PubMed:27551070}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01185}.
CC -!- SIMILARITY: Belongs to the FliW family. {ECO:0000255|HAMAP-
CC Rule:MF_01185}.
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DR EMBL; CP000557; ABO68404.1; -; Genomic_DNA.
DR RefSeq; WP_011888205.1; NC_009328.1.
DR PDB; 5DMB; X-ray; 2.30 A; A=2-144.
DR PDB; 5DMD; X-ray; 1.45 A; A/B=2-144.
DR PDB; 5JAK; X-ray; 1.80 A; A=2-144.
DR PDBsum; 5DMB; -.
DR PDBsum; 5DMD; -.
DR PDBsum; 5JAK; -.
DR AlphaFoldDB; A4ISV0; -.
DR SMR; A4ISV0; -.
DR STRING; 420246.GTNG_3059; -.
DR EnsemblBacteria; ABO68404; ABO68404; GTNG_3059.
DR KEGG; gtn:GTNG_3059; -.
DR eggNOG; COG1699; Bacteria.
DR HOGENOM; CLU_112356_0_2_9; -.
DR OMA; DVAVFCI; -.
DR OrthoDB; 1767625at2; -.
DR Proteomes; UP000001578; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0044780; P:bacterial-type flagellum assembly; IEA:UniProtKB-UniRule.
DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW.
DR Gene3D; 2.30.290.10; -; 1.
DR HAMAP; MF_01185; FliW; 1.
DR InterPro; IPR003775; Flagellar_assembly_factor_FliW.
DR InterPro; IPR024046; Flagellar_assmbl_FliW_dom_sf.
DR PANTHER; PTHR39190; PTHR39190; 1.
DR Pfam; PF02623; FliW; 1.
DR SUPFAM; SSF141457; SSF141457; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Bacterial flagellum biogenesis; Chaperone; Cytoplasm;
KW Translation regulation.
FT CHAIN 1..144
FT /note="Flagellar assembly factor FliW"
FT /id="PRO_1000065818"
FT MUTAGEN 44
FT /note="F->D: Loss of interaction with CsrA."
FT /evidence="ECO:0000269|PubMed:27551070"
FT MUTAGEN 123
FT /note="Q->D: Loss of interaction with CsrA."
FT /evidence="ECO:0000269|PubMed:27551070"
FT MUTAGEN 125
FT /note="I->D: Loss of interaction with CsrA."
FT /evidence="ECO:0000269|PubMed:27551070"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 10..12
FT /evidence="ECO:0007829|PDB:5DMD"
FT HELIX 15..17
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 33..38
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 40..43
FT /evidence="ECO:0007829|PDB:5JAK"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5DMD"
FT HELIX 62..64
FT /evidence="ECO:0007829|PDB:5DMD"
FT HELIX 75..80
FT /evidence="ECO:0007829|PDB:5DMD"
FT HELIX 86..88
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:5DMD"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:5DMD"
FT TURN 116..119
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:5DMD"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5DMD"
SQ SEQUENCE 144 AA; 16456 MW; 01ECB0352571F308 CRC64;
MKIATKYHGD IEIHEKDIVR FEQGIPGFLE EKQFVLLPLE DTPFIILQSV NTPALGFVLI
EPFSYFPTYE IDLDDNTLEQ LQITGEQDVA LYVILTVADP FDDTTANLQA PIVINVHKRL
GKQVILTNTN YKTKHRLFPE KVAK
