ID   FLIF_CERSP              Reviewed;         570 AA.
AC   Q53151;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Flagellar M-ring protein;
GN   Name=fliF;
OS   Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=1063;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=WS8;
RA   Goodfellow I.G., Woolley K.J., Sockett R.E.S.;
RL   Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The M ring may be actively involved in energy transduction.
CC       {ECO:0000250}.
CC   -!- SUBUNIT: The basal body constitutes a major portion of the flagellar
CC       organelle and consists of four rings (L,P,S, and M) mounted on a
CC       central rod. The M ring is integral to the inner membrane of the cell
CC       and may be connected to the flagellar rod via the S ring. The S
CC       (supramembrane ring) lies just distal to the M ring. The L and P rings
CC       lie in the outer membrane and the periplasmic space, respectively (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Bacterial flagellum basal body
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FliF family. {ECO:0000305}.
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DR   EMBL; X98692; CAA67251.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q53151; -.
DR   SMR; Q53151; -.
DR   GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; IEA:InterPro.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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   PANTHER; PTHR30046; PTHR30046; 1.
DR   PANTHER; PTHR30046:SF0; PTHR30046:SF0; 1.
DR   Pfam; PF01514; YscJ_FliF; 1.
DR   Pfam; PF08345; YscJ_FliF_C; 1.
DR   PIRSF; PIRSF004862; FliF; 1.
DR   PRINTS; PR01009; FLGMRINGFLIF.
DR   TIGRFAMs; TIGR00206; fliF; 1.
PE   3: Inferred from homology;
KW   Bacterial flagellum; Cell inner membrane; Cell membrane; Membrane;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..570
FT                   /note="Flagellar M-ring protein"
FT                   /id="PRO_0000180886"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        463..483
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          312..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  60676 MW;  87A6BF11C3DA6A46 CRC64;
     MAPSPTPPAV RRPASALIPQ MRGMLDQIRR FGDQPGLRRA MPAILILAVT VLALAGWILL
     REPARVTLYP GLPEAEKARV IDSLTGGGIA AVIDERTGEV AVPGAEYHRA RMLLAAQGLP
     QGLPDGNALL SDLPMGTSKS VETARLRQAQ ELDLARSITE ISAVSAARVH LALPERSAFL
     RESQPPRASV FLQIVPGRTL DGAQVEAIVN LVSSSVPGMA RQDVTVVDQM GRLLSRGSDD
     PAVLLNDRQL QHRVQLETLY RNRIESLLTP IAGPGNLAVQ VTIDMDFTRQ EIREEQVDPD
     RTALLAEQSQ IEETADPQAR GIPGAVSNSP PPEAALEAGA PPTAAGEAAA PMRSRSQNST
     RNFEVSRKVE TTLPATARIA RVSAAVVVRA QPQPAATDPA APPPPLLPEA LKADLERLTR
     SAVGFDADRG DVVTITAQPF LDTVVPEASG WSAEPWVADL ARQGFLLAAL AVVALGVVRP
     ILNRVLLPAP AAAGALPLGE TAVEVGEGES LDDVRARLKA RQGALTKNML DAARSHEEQI
     LVIRKLVEED EGRIATTIRQ MIAAELDTVK