ID Q07T10_RHOP5 Unreviewed; 116 AA.
AC Q07T10;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|ARBA:ARBA00021897, ECO:0000256|RuleBase:RU362074};
GN OrderedLocusNames=RPE_0968 {ECO:0000313|EMBL:ABJ04924.1};
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316055 {ECO:0000313|EMBL:ABJ04924.1};
RN [1] {ECO:0000313|EMBL:ABJ04924.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53 {ECO:0000313|EMBL:ABJ04924.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: FliN is one of three proteins (FliG, FliN, FliM) that form
CC the rotor-mounted switch complex (C ring), located at the base of the
CC basal body. This complex interacts with the CheY and CheZ chemotaxis
CC proteins, in addition to contacting components of the motor that
CC determine the direction of flagellar rotation.
CC {ECO:0000256|RuleBase:RU362074}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362074};
CC Peripheral membrane protein {ECO:0000256|RuleBase:RU362074};
CC Cytoplasmic side {ECO:0000256|RuleBase:RU362074}. Bacterial flagellum
CC basal body {ECO:0000256|RuleBase:RU362074}. Membrane
CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004287}.
CC -!- SIMILARITY: Belongs to the FliN/MopA/SpaO family.
CC {ECO:0000256|ARBA:ARBA00009226, ECO:0000256|RuleBase:RU362074}.
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DR EMBL; CP000463; ABJ04924.1; -; Genomic_DNA.
DR AlphaFoldDB; Q07T10; -.
DR STRING; 316055.RPE_0968; -.
DR KEGG; rpe:RPE_0968; -.
DR eggNOG; COG1886; Bacteria.
DR HOGENOM; CLU_097058_5_1_5; -.
DR OrthoDB; 9790303at2; -.
DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:UniProtKB-UniRule.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR Gene3D; 2.30.330.10; SpoA-like; 1.
DR InterPro; IPR012826; FliN.
DR InterPro; IPR001543; FliN-like_C.
DR InterPro; IPR001172; FliN_T3SS_HrcQb.
DR InterPro; IPR036429; SpoA-like_sf.
DR NCBIfam; TIGR02480; fliN; 1.
DR PANTHER; PTHR43484; -; 1.
DR PANTHER; PTHR43484:SF1; FLAGELLAR MOTOR SWITCH PROTEIN FLIN; 1.
DR Pfam; PF01052; FliMN_C; 1.
DR PRINTS; PR00956; FLGMOTORFLIN.
DR SUPFAM; SSF101801; Surface presentation of antigens (SPOA); 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|RuleBase:RU362074};
KW Cell membrane {ECO:0000256|RuleBase:RU362074};
KW Cell projection {ECO:0000313|EMBL:ABJ04924.1};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW Cilium {ECO:0000313|EMBL:ABJ04924.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW Flagellum {ECO:0000313|EMBL:ABJ04924.1};
KW Membrane {ECO:0000256|RuleBase:RU362074}.
FT DOMAIN 41..111
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 116 AA; 12505 MW; 5222EA429FC91007 CRC64;
MADNDTKVPL PDLNSGDVPA MTDVDYNDEE HASRVAADLE AVFDVPVQVS AVLGRSKMDV
GELLKLGPGT VLELDRKVGE AIDIYVNNRL IARGEVVLVE DKLGVTMTEI IAAERT
//