ID A0A1H7SMA8_9BURK Unreviewed; 327 AA.
AC A0A1H7SMA8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Flagellar motor switch protein FliM {ECO:0000256|ARBA:ARBA00021898};
GN ORFNames=SAMN05216319_2562 {ECO:0000313|EMBL:SEL73519.1};
OS Duganella sp. CF402.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1855289 {ECO:0000313|EMBL:SEL73519.1, ECO:0000313|Proteomes:UP000198529};
RN [1] {ECO:0000313|Proteomes:UP000198529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF402 {ECO:0000313|Proteomes:UP000198529};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOBG01000001; SEL73519.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H7SMA8; -.
DR STRING; 1855289.SAMN05216319_2562; -.
DR Proteomes; UP000198529; 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:SEL73519.1};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cilium {ECO:0000313|EMBL:SEL73519.1};
KW Flagellar rotation {ECO:0000256|ARBA:ARBA00022779};
KW Flagellum {ECO:0000313|EMBL:SEL73519.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 250..318
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
SQ SEQUENCE 327 AA; 36715 MW; 8C1124285E3AFD71 CRC64;
MADNFLSQEE VDALLKGVNG DQDDVAAQED VAGVRTYNLA TQERIVRGRM PTLEIINERF
ARLLRVGLFN FLRRSAEVSV GSVRVSKYSE FIRNLVVPTN LNLVHMKPLR GTALMVFDPG
LVFLLVDNLF GGDGRFHTRV EGRDFTQTEQ RIILRILDIV FEAYTKSWEP VYPVEFEYIR
SEMNTQFANI ATPNEVVVAS TFTVELGSVS GQIHFCMPYS MIEPIRDSLT SSLQGEALEV
DKRWIRLMTQ QIQIAEVEVV ASLGTAKVNF DEILNMRVGD IIPLTIPELI SATVDGVPVM
DCSYGVMNGQ YALKVEKLLA NTDNLKN
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