ID A0A1W2AB83_9SPHN Unreviewed; 101 AA.
AC A0A1W2AB83;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|ARBA:ARBA00021897, ECO:0000256|RuleBase:RU362074};
GN ORFNames=SAMN06272759_104249 {ECO:0000313|EMBL:SMC57937.1};
OS Novosphingobium sp. B1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1938756 {ECO:0000313|EMBL:SMC57937.1, ECO:0000313|Proteomes:UP000192500};
RN [1] {ECO:0000313|Proteomes:UP000192500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1 {ECO:0000313|Proteomes:UP000192500};
RA Varghese N., Submissions S.;
RL Submitted (APR-2017) 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; FWXL01000004; SMC57937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2AB83; -.
DR STRING; 1938756.SAMN06272759_104249; -.
DR OrthoDB; 9790303at2; -.
DR Proteomes; UP000192500; 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:SMC57937.1};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW Cilium {ECO:0000313|EMBL:SMC57937.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW Flagellum {ECO:0000313|EMBL:SMC57937.1};
KW Membrane {ECO:0000256|RuleBase:RU362074}.
FT DOMAIN 11..79
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
SQ SEQUENCE 101 AA; 10962 MW; 0496522EC1925E0E CRC64;
MTFQPRGFDF LKDVDVRLTV ELGRTSMTLK DVLGLTEESV VMLDRLTDEL LDVMVNGKLI
ARGEVVAQGD RFGLRIVELA GAEAEETPAL PARKSAKGGD A
//
