ID A0A1G5MV10_AFIMA Unreviewed; 125 AA.
AC A0A1G5MV10;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|ARBA:ARBA00021897, ECO:0000256|RuleBase:RU362074};
GN ORFNames=SAMN03080610_01059 {ECO:0000313|EMBL:SCZ28902.1};
OS Afifella marina DSM 2698.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Afifellaceae; Afifella.
OX NCBI_TaxID=1120955 {ECO:0000313|EMBL:SCZ28902.1, ECO:0000313|Proteomes:UP000199347};
RN [1] {ECO:0000313|EMBL:SCZ28902.1, ECO:0000313|Proteomes:UP000199347}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2698 {ECO:0000313|EMBL:SCZ28902.1,
RC ECO:0000313|Proteomes:UP000199347};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FMVW01000002; SCZ28902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5MV10; -.
DR STRING; 1120955.SAMN03080610_01059; -.
DR OrthoDB; 9790303at2; -.
DR Proteomes; UP000199347; 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:SCZ28902.1};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW Cilium {ECO:0000313|EMBL:SCZ28902.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW Flagellum {ECO:0000313|EMBL:SCZ28902.1};
KW Membrane {ECO:0000256|RuleBase:RU362074};
KW Reference proteome {ECO:0000313|Proteomes:UP000199347}.
FT DOMAIN 43..116
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 125 AA; 13322 MW; 2C44FBE547B669DA CRC64;
MSGDPLKDMQ EKLDETATHQ DDFTVDVPAG QGETFGTGRN LESVMRIPVL MQVVLGSARM
PVANLMKLGR GAIVPLDHRV GEPVEVVVNG RVIARGEVVV VEDDNSRFGV SLTEIVGPAG
AELTN
//