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Database: UniProt
Entry: A0A432W4T1_9GAMM
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Original site: A0A432W4T1_9GAMM 
ID   A0A432W4T1_9GAMM        Unreviewed;       145 AA.
AC   A0A432W4T1;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Flagellar motor switch protein FliN {ECO:0000256|ARBA:ARBA00021897, ECO:0000256|RuleBase:RU362074};
GN   Name=fliN {ECO:0000313|EMBL:RUO24513.1};
GN   ORFNames=CWE09_11725 {ECO:0000313|EMBL:RUO24513.1};
OS   Aliidiomarina minuta.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Aliidiomarina.
OX   NCBI_TaxID=880057 {ECO:0000313|EMBL:RUO24513.1, ECO:0000313|Proteomes:UP000288293};
RN   [1] {ECO:0000313|EMBL:RUO24513.1, ECO:0000313|Proteomes:UP000288293}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MLST1 {ECO:0000313|EMBL:RUO24513.1,
RC   ECO:0000313|Proteomes:UP000288293};
RX   PubMed=30364313; DOI=.3389/fmicb.2018.02453;
RA   Liu Y., Lai Q., Shao Z.;
RT   "Genome-Based Analysis Reveals the Taxonomy and Diversity of the Family
RT   Idiomarinaceae.";
RL   Front. Microbiol. 9:2453-2453(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:RUO24513.1}.
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DR   EMBL; PIPL01000002; RUO24513.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A432W4T1; -.
DR   OrthoDB; 9773459at2; -.
DR   Proteomes; UP000288293; 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:RUO24513.1};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500, ECO:0000256|RuleBase:RU362074};
KW   Cilium {ECO:0000313|EMBL:RUO24513.1};
KW   Flagellar rotation {ECO:0000256|RuleBase:RU362074};
KW   Flagellum {ECO:0000313|EMBL:RUO24513.1};
KW   Membrane {ECO:0000256|RuleBase:RU362074};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288293}.
FT   DOMAIN          65..135
FT                   /note="Flagellar motor switch protein FliN-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01052"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..32
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        33..62
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   145 AA;  16239 MW;  6C3EFF3A09CA72DC CRC64;
     MSDKDDNDTH DEMDDWEAAM AEQEDTEKAE DEVEGDNVLG AKRAELEELS DDSNQSPEER
     RKLDAILDIP VTISMEVGRS QISIRNLLQL NQGSVVELER VAGEPLDVLV NGTLIAHGEV
     VVVNDKFGIR LTDVISQLER IRKLR
//
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