ID   FLIF_AQUAE              Reviewed;         489 AA.
AC   O67241;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Flagellar M-ring protein;
GN   Name=fliF; OrderedLocusNames=aq_1182;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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 five rings (E,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; AE000657; AAC07196.1; -; Genomic_DNA.
DR   PIR; F70401; F70401.
DR   RefSeq; NP_213805.1; NC_000918.1.
DR   RefSeq; WP_010880743.1; NC_000918.1.
DR   PDB; 7CIK; X-ray; 2.29 A; A/B=58-213.
DR   PDBsum; 7CIK; -.
DR   AlphaFoldDB; O67241; -.
DR   SMR; O67241; -.
DR   STRING; 224324.aq_1182; -.
DR   EnsemblBacteria; AAC07196; AAC07196; aq_1182.
DR   KEGG; aae:aq_1182; -.
DR   PATRIC; fig|224324.8.peg.918; -.
DR   eggNOG; COG1766; Bacteria.
DR   HOGENOM; CLU_028108_2_0_0; -.
DR   InParanoid; O67241; -.
DR   OMA; NYEVNRI; -.
DR   OrthoDB; 167675at2; -.
DR   Proteomes; UP000000798; Chromosome.
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   1: Evidence at protein level;
KW   3D-structure; Bacterial flagellum; Cell inner membrane; Cell membrane;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..489
FT                   /note="Flagellar M-ring protein"
FT                   /id="PRO_0000180872"
FT   TRANSMEM        24..44
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        412..432
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          290..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        300..315
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           62..68
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   TURN            69..72
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          79..82
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          84..87
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   HELIX           88..101
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          108..114
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          116..121
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   HELIX           123..142
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          145..156
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          171..178
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   HELIX           186..197
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   HELIX           205..207
FT                   /evidence="ECO:0007829|PDB:7CIK"
FT   STRAND          208..212
FT                   /evidence="ECO:0007829|PDB:7CIK"
SQ   SEQUENCE   489 AA;  54450 MW;  BFB5F2BBF5CC9211 CRC64;
     MDKLREYLNL LKERFNALTP VQKALAVGIP LLLLSLGAVA LIYLSQENYT VLYTGLSPDD
     LNAVVTELDK EGVKYKISPD GRTIYVPENV ARELRLKLAA KGVPRKGIVG YELFDKSGIV
     LSRFQQLVNF KRAIEGELAK TIMSLDCVEF ARVHIVLPEK SLFIREEEEA KASVFLKLKP
     GCELTPEQVK AIRNLVSGSV ENLKPSQVVV VDDKGRDLTA YLDEEFKTNA SQLKVKREFE
     KSLERKLQKT LEEVFGYGKV KVNVSAELDF SSMKKREELY DPDLTAVVSE QKKKERTTST
     RAQGIPGTQA NIPPATGRQG GGELITERKE SITNYEVSKR EIYFEDKTIK VKRISVGLVI
     DKDVKVNTEE LKNLIIASAG LDPKRGDQVS IVSVPFVKPT VVAEKPKVPT YVYVAVALVS
     LVILGLVAFG LVKLLRRRPP APTPAPAVPG VPPTVEEVRK KTPYEELLEI AKQEPEKVAM
     VLKKWLKEG