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Database: UniProt
Entry: A0A3M0BJ79_9AQUI
LinkDB: A0A3M0BJ79_9AQUI
Original site: A0A3M0BJ79_9AQUI 
ID   A0A3M0BJ79_9AQUI        Unreviewed;       198 AA.
AC   A0A3M0BJ79;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|RuleBase:RU362074};
GN   ORFNames=CLV39_0116 {ECO:0000313|EMBL:RMA97503.1};
OS   Hydrogenothermus marinus.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Hydrogenothermus.
OX   NCBI_TaxID=133270 {ECO:0000313|EMBL:RMA97503.1, ECO:0000313|Proteomes:UP000280842};
RN   [1] {ECO:0000313|EMBL:RMA97503.1, ECO:0000313|Proteomes:UP000280842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VM1 {ECO:0000313|EMBL:RMA97503.1,
RC   ECO:0000313|Proteomes:UP000280842};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-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:RMA97503.1}.
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DR   EMBL; REFO01000010; RMA97503.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M0BJ79; -.
DR   OrthoDB; 9773459at2; -.
DR   Proteomes; UP000280842; 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:RMA97503.1};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW   Cilium {ECO:0000313|EMBL:RMA97503.1};
KW   Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW   Flagellum {ECO:0000313|EMBL:RMA97503.1};
KW   Membrane {ECO:0000256|RuleBase:RU362074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280842}.
FT   DOMAIN          113..183
FT                   /note="Flagellar motor switch protein FliN-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01052"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  22796 MW;  6368470FFF4F7557 CRC64;
     MAEENQNINP EEESSKQEQE NQDLNQEDLA KQWEESLQQQ EKKQEGSSDE NQEDLAKQWE
     EALQQQNEES NDNQEDIAKQ WEESLQQEEG KPTEKENIQG INIPGIDNEK LEMLLDIPLE
     ISVEVGNKTL TLEDILKLNS NAIVELDRYI NEPVDIKING KLIAKGELYT VENNFGIKIT
     NIVTVQERLK FLMENGGE
//
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