ID B2UJT7_RALPJ Unreviewed; 335 AA.
AC B2UJT7;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Flagellar motor switch protein FliM {ECO:0000256|ARBA:ARBA00021898};
GN OrderedLocusNames=Rpic_4754 {ECO:0000313|EMBL:ACD29838.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29838.1};
RN [1] {ECO:0000313|EMBL:ACD29838.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=12J {ECO:0000313|EMBL:ACD29838.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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; CP001069; ACD29838.1; -; Genomic_DNA.
DR AlphaFoldDB; B2UJT7; -.
DR STRING; 402626.Rpic_4754; -.
DR KEGG; rpi:Rpic_4754; -.
DR PATRIC; fig|402626.5.peg.999; -.
DR eggNOG; COG1868; Bacteria.
DR HOGENOM; CLU_052646_1_2_4; -.
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:ACD29838.1};
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cilium {ECO:0000313|EMBL:ACD29838.1};
KW Flagellar rotation {ECO:0000256|ARBA:ARBA00022779};
KW Flagellum {ECO:0000313|EMBL:ACD29838.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 251..320
FT /note="Flagellar motor switch protein FliN-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF01052"
SQ SEQUENCE 335 AA; 38072 MW; B4B726973FB8156E CRC64;
MLKEEFLSQE EIDALLKGVS DEADEEPVEA DPSGIRTYNL GSQERIVRGR MPTLEIINER
FARNWRIGLF NFMRRNAEIS VGPVKVQKYS EFIRNLVVPT SLNLVHVKPL RGTALFVFDP
NLIFLVVDNL FGGDGRFHMR VEGRDFTDVE QRIIQRMLQL VFEHYARAWQ PVYPIDFEFL
RMEMHTEFAN VATPNEVVVT TTFSLELGNN GGDVHICMPY TMIEPIRDRL TSAIQGEALE
VDKRWLRLLS QQVQTAEVEL IADLATANVQ VSDILNMKVG DVIPLELDDV VTAKVDGVPV
MECNYGTFNG QYALRVNRML NMSGSEPATE SDDDN
//
