ID Q132C2_RHOPS Unreviewed; 532 AA.
AC Q132C2;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE RecName: Full=Flagellar M-ring protein {ECO:0000256|PIRNR:PIRNR004862};
GN OrderedLocusNames=RPD_3846 {ECO:0000313|EMBL:ABE41067.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE41067.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE41067.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE41067.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The M ring may be actively involved in energy transduction.
CC {ECO:0000256|PIRNR:PIRNR004862}.
CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC {ECO:0000256|ARBA:ARBA00004117, ECO:0000256|PIRNR:PIRNR004862}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FliF family. {ECO:0000256|ARBA:ARBA00007971,
CC ECO:0000256|PIRNR:PIRNR004862}.
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DR EMBL; CP000283; ABE41067.1; -; Genomic_DNA.
DR AlphaFoldDB; Q132C2; -.
DR STRING; 316057.RPD_3846; -.
DR KEGG; rpd:RPD_3846; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_4_1_5; -.
DR OMA; NYEVNRI; -.
DR BioCyc; RPAL316057:RPD_RS19330-MONOMER; -.
DR Proteomes; UP000001818; Chromosome.
DR GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; IEA:InterPro.
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 Gene3D; 3.30.300.30; -; 1.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR013556; Flag_M-ring_C.
DR InterPro; IPR000067; FlgMring_FliF.
DR InterPro; IPR006182; FliF_N_dom.
DR InterPro; IPR043427; YscJ/FliF.
DR NCBIfam; TIGR00206; fliF; 1.
DR PANTHER; PTHR30046; FLAGELLAR M-RING PROTEIN; 1.
DR PANTHER; PTHR30046:SF0; FLAGELLAR M-RING PROTEIN; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR Pfam; PF08345; YscJ_FliF_C; 1.
DR PIRSF; PIRSF004862; FliF; 1.
DR PRINTS; PR01009; FLGMRINGFLIF.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143,
KW ECO:0000256|PIRNR:PIRNR004862};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000313|EMBL:ABE41067.1};
KW Cilium {ECO:0000313|EMBL:ABE41067.1};
KW Flagellum {ECO:0000313|EMBL:ABE41067.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 430..451
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..211
FT /note="Flagellar M-ring N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01514"
FT DOMAIN 246..404
FT /note="Flagellar M-ring C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08345"
FT REGION 268..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..317
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 532 AA; 57846 MW; 292CB3CC81B18073 CRC64;
MQSLLGFLKG LGAARVMAMI AVTVALLGFF AFVIMRVSQP QMTTLYTDLS VEDSSSIIKE
LERQAIPFEM RNEGTTLMVP KDKVTRLRMK LAEGGLPKGG GVGYEIFDKS DALGTTSFVQ
NINHLRALEG ELARTIRAID RIQQARVHLV LPERPLFSRE TPEPSASIVL RVRGALEPQQ
VRAIRHLVAS AVNGLKPQRV SIVDEGGQLL ADGSASANAA DGAAGDERRT SFEKRMRNEI
EGIVSSVVGS GRARVQVTAD FDYNKITQTS DKFDPEGRVL RSSQTREEQS QTSAADGQVT
VNNELPGNQG QAGTGPRDQS KKSEETNNYE ISRITKTEVT EAGRVNRLSV AVLVDGIYTK
NEKGELVYAE RPKEQLDRIA ALVRSAIGFD QKRGDQIEVV NLKFAEAPQV EKLPEQAGLL
GMFQFTKDDI MNMIQLGVML VLGLVVLFMV IRPLVKRVLA SDPGPEGPGL PALTDGSVPQ
IGADGQPQPS MIDIAQVQGQ VHAQSVHRVG ELADRNPNET AAIVRQWLAE PA
//