FLIW_TREPA
ID FLIW_TREPA Reviewed; 150 AA.
AC O83664;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Flagellar assembly factor FliW {ECO:0000255|HAMAP-Rule:MF_01185, ECO:0000303|PubMed:16936039};
GN Name=fliW {ECO:0000255|HAMAP-Rule:MF_01185, ECO:0000303|PubMed:16936039};
GN OrderedLocusNames=TP_0658;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
RN [2]
RP FUNCTION, AND INTERACTION WITH FLAGELLINS.
RC STRAIN=Nichols;
RX PubMed=16936039; DOI=10.1128/jb.00820-06;
RA Titz B., Rajagopala S.V., Ester C., Haeuser R., Uetz P.;
RT "Novel conserved assembly factor of the bacterial flagellum.";
RL J. Bacteriol. 188:7700-7706(2006).
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: Binds to the C-terminal region of flagellin, which is
CC implicated in polymerization, and participates in the assembly of the
CC flagellum (PubMed:16936039). {ECO:0000269|PubMed:16936039}.
CC -!- SUBUNIT: Interacts with translational regulator CsrA (By similarity).
CC Interacts with flagellins FlaB1, FlaB2 and FlaB3.
CC {ECO:0000250|UniProtKB:P96503, ECO:0000269|PubMed:16936039}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01185,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the FliW family. {ECO:0000255|HAMAP-
CC Rule:MF_01185, ECO:0000305}.
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DR EMBL; AE000520; AAC65632.1; -; Genomic_DNA.
DR PIR; C71297; C71297.
DR RefSeq; WP_010882103.1; NC_021490.2.
DR AlphaFoldDB; O83664; -.
DR SMR; O83664; -.
DR IntAct; O83664; 11.
DR STRING; 243276.TPANIC_0658; -.
DR EnsemblBacteria; AAC65632; AAC65632; TP_0658.
DR GeneID; 57879181; -.
DR KEGG; tpa:TP_0658; -.
DR eggNOG; COG1699; Bacteria.
DR HOGENOM; CLU_112356_0_2_12; -.
DR OMA; DVAVFCI; -.
DR OrthoDB; 1767625at2; -.
DR Proteomes; UP000000811; 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 Bacterial flagellum biogenesis; Chaperone; Cytoplasm; Reference proteome;
KW Translation regulation.
FT CHAIN 1..150
FT /note="Flagellar assembly factor FliW"
FT /id="PRO_0000273014"
SQ SEQUENCE 150 AA; 16925 MW; 8DEB1A015C5437AC CRC64;
MEIQTKTLGT QTVEAHQIIT LERGLYGFEK YHRFALFDAV QVPFIHMQSL DDPALSFIAI
DPFLFRPDYE LDIDDVLLQP LDISSPTDVL VFALVTIPPD GSAVTANLQG PLIVNKKNRK
AMQVAMGGDR WRTKHDIVAE MAERRAQEQC
