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Database: UniProt
Entry: A0A1H2PJM0_9BURK
LinkDB: A0A1H2PJM0_9BURK
Original site: A0A1H2PJM0_9BURK 
ID   A0A1H2PJM0_9BURK        Unreviewed;       331 AA.
AC   A0A1H2PJM0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Flagellar motor switch protein FliM {ECO:0000256|ARBA:ARBA00021898};
GN   ORFNames=SAMN05216551_101462 {ECO:0000313|EMBL:SDV46589.1};
OS   Chitinasiproducens palmae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Chitinasiproducens.
OX   NCBI_TaxID=1770053 {ECO:0000313|EMBL:SDV46589.1, ECO:0000313|Proteomes:UP000243719};
RN   [1] {ECO:0000313|Proteomes:UP000243719}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS23 {ECO:0000313|Proteomes:UP000243719};
RA   Varghese N., Submissions S.;
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: FliM is one of three proteins (FliG, FliN, FliM) that forms
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|ARBA:ARBA00025044}.
CC   -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC       {ECO:0000256|ARBA:ARBA00004117}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the FliM family.
CC       {ECO:0000256|ARBA:ARBA00011049}.
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DR   EMBL; FNLO01000001; SDV46589.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H2PJM0; -.
DR   STRING; 1770053.SAMN05216551_101462; -.
DR   OrthoDB; 9806941at2; -.
DR   Proteomes; UP000243719; 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-KW.
DR   GO; GO:0003774; F:cytoskeletal motor activity; IEA:InterPro.
DR   GO; GO:0071973; P:bacterial-type flagellum-dependent cell motility; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   CDD; cd17908; FliM; 1.
DR   Gene3D; 3.40.1550.10; CheC-like; 1.
DR   Gene3D; 2.30.330.10; SpoA-like; 1.
DR   InterPro; IPR028976; CheC-like_sf.
DR   InterPro; IPR001689; Flag_FliM.
DR   InterPro; IPR001543; FliN-like_C.
DR   InterPro; IPR036429; SpoA-like_sf.
DR   NCBIfam; TIGR01397; fliM_switch; 1.
DR   PANTHER; PTHR30034; FLAGELLAR MOTOR SWITCH PROTEIN FLIM; 1.
DR   PANTHER; PTHR30034:SF3; FLAGELLAR MOTOR SWITCH PROTEIN FLIM; 1.
DR   Pfam; PF02154; FliM; 1.
DR   Pfam; PF01052; FliMN_C; 1.
DR   PIRSF; PIRSF002888; FliM; 1.
DR   PRINTS; PR00955; FLGMOTORFLIM.
DR   SUPFAM; SSF103039; CheC-like; 1.
DR   SUPFAM; SSF101801; Surface presentation of antigens (SPOA); 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143};
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell projection {ECO:0000313|EMBL:SDV46589.1};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Cilium {ECO:0000313|EMBL:SDV46589.1};
KW   Flagellar rotation {ECO:0000256|ARBA:ARBA00022779};
KW   Flagellum {ECO:0000313|EMBL:SDV46589.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243719}.
FT   DOMAIN          251..320
FT                   /note="Flagellar motor switch protein FliN-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01052"
SQ   SEQUENCE   331 AA;  37062 MW;  345970C4A0C201AD CRC64;
     MSQEEFLSQE EVDALLKGVT GEADAAPETP LAGGVRPYDL ATQERIVRGR MPTLEIINER
     FARLLRAGIF NFMRRSAEIS VGPVKVQKYS EFIRNLPVPT NLNLIHIKPL RGTALFIFDP
     QLIFLVVDTL FGGDGRFHMR VEGRDFTPTE QRIIRKLVNL VLENYGASWK PVFPVEFQYV
     RAELHTQFAN VATPNEVVVS TSFAIEFGAQ GGNLHICTPY SMIEPVRDLL SSPLQGEALE
     VDKRWVRLLS QQVQAAEVEL QVDLAQIRTT FRDIVGMRAG DVIPIDMPET VTAKVDGVPV
     MDCTYGIFNG QYALRVSRMI GSTDSKENGY D
//
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