ID A0A2S6MUY9_RHOGL Unreviewed; 104 AA.
AC A0A2S6MUY9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|ARBA:ARBA00021897, ECO:0000256|RuleBase:RU362074};
GN ORFNames=CCS01_30605 {ECO:0000313|EMBL:PPQ26180.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ26180.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ26180.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ26180.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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}.
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:PPQ26180.1}.
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DR EMBL; NHRY01000272; PPQ26180.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6MUY9; -.
DR OrthoDB; 9790303at2; -.
DR Proteomes; UP000239724; Unassembled WGS sequence.
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:PPQ26180.1};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW Cilium {ECO:0000313|EMBL:PPQ26180.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW Flagellum {ECO:0000313|EMBL:PPQ26180.1};
KW Membrane {ECO:0000256|RuleBase:RU362074};
KW Reference proteome {ECO:0000313|Proteomes:UP000239724}.
FT DOMAIN 28..99
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 104 AA; 11371 MW; 126D164877B85FBF CRC64;
MPGPDQTQTP TQEPAETSEI GYPKELEAVY DISVTVSAVL GKATMQVNQL LKLGRGAVVE
LDRKLGEAID IYVNNRLIAR GEVVMVDDVK LGITMTEIVK SERQ
//
