ID A0A3P1SQA2_9GAMM Unreviewed; 135 AA.
AC A0A3P1SQA2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|ARBA:ARBA00021897, ECO:0000256|RuleBase:RU362074};
GN Name=fliN {ECO:0000313|EMBL:RRC99229.1};
GN ORFNames=EHS89_10280 {ECO:0000313|EMBL:RRC99229.1};
OS Amphritea balenae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Amphritea.
OX NCBI_TaxID=452629 {ECO:0000313|EMBL:RRC99229.1, ECO:0000313|Proteomes:UP000267535};
RN [1] {ECO:0000313|EMBL:RRC99229.1, ECO:0000313|Proteomes:UP000267535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JAMM 1525 {ECO:0000313|EMBL:RRC99229.1,
RC ECO:0000313|Proteomes:UP000267535};
RA Fang Z., Zhang Y., Han X.;
RT "The draft genome sequence of Amphritea balenae JAMM 1525T.";
RL Submitted (NOV-2018) 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}.
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:RRC99229.1}.
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DR EMBL; RQXV01000005; RRC99229.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P1SQA2; -.
DR OrthoDB; 9773459at2; -.
DR Proteomes; UP000267535; 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:RRC99229.1};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW Cilium {ECO:0000313|EMBL:RRC99229.1};
KW Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW Flagellum {ECO:0000313|EMBL:RRC99229.1};
KW Membrane {ECO:0000256|RuleBase:RU362074}.
FT DOMAIN 56..125
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 135 AA; 14672 MW; 0822F59D1CE5924F CRC64;
MSEEEIEGQE QGGDDWGAAM AEQAQSEVAG AEGQSVDLDE LRDDSLPLNN PSLDVVLDIP
VKLSMEVGRA DIPIRNLLQL NQGSVVELDR VAGEPLDVMV NGTLIAHGEV VVVNDRYGIR
LTDVISPQER IEKLR
//
