ID   FLIF_BRUSU              Reviewed;         580 AA.
AC   Q8FUS3; G0KEE3;
DT   07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=Flagellar M-ring protein FliF;
GN   Name=fliF; OrderedLocusNames=BRA1146, BS1330_II1137;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
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}.
CC   -!- CAUTION: Brucella species display species-specific inactivation of
CC       flagellar genes and are consequently nonmotile. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE014292; AAN34305.1; -; Genomic_DNA.
DR   EMBL; CP002998; AEM20581.1; -; Genomic_DNA.
DR   RefSeq; WP_002966637.1; NZ_KN046805.1.
DR   AlphaFoldDB; Q8FUS3; -.
DR   SMR; Q8FUS3; -.
DR   EnsemblBacteria; AEM20581; AEM20581; BS1330_II1137.
DR   GeneID; 45126407; -.
DR   KEGG; bms:BRA1146; -.
DR   KEGG; bsi:BS1330_II1137; -.
DR   HOGENOM; CLU_028108_4_0_5; -.
DR   OMA; ITTRPHY; -.
DR   PRO; PR:Q8FUS3; -.
DR   Proteomes; UP000007104; Chromosome II.
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..580
FT                   /note="Flagellar M-ring protein FliF"
FT                   /id="PRO_0000180877"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        445..465
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          273..341
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        307..330
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  62168 MW;  735D676BEA8FB030 CRC64;
     MAVVWMQQNF QQLIEQLKGT LGKLGARKLI ALGLVGAALM GAILYTSIYL GRPSYETLYV
     GLSRDDVNRM GLALGEAGIP FDVKSDGSSI LVPIGKAENA RMYLAEKGLP TSNNAGYELF
     DNMGSLGLTS FMQEITRVRA LEGEIARTIQ AIRGVKAARV HIVLAEKGSF RRGDQKPSAS
     VVIRAEGGFS AESAQSIRQL VAAAVPSLDA SSVTVLDTNG HLLASAGEGA NGAALMTASL
     EQQVASHVDD SIRKALAPYL GLGHFQTSVQ AALDTDRRQT KETTYDPESR VERSVRVVRE
     SGDSRNNRND NATGVEQNIP QEQIQNRNGE SSTEKTDRRE ELTNYEVNSK TVSTVSDGYS
     IKRLSIAVVI DQARLLQTAG TTPPPANFVD QQITKIRDLV ATAAGLNTNR GDVINVTAVN
     FLDPAGADME PVSAPWTDTL LRQSGSYANA LAILAAVGLL IWFGLRPLLR DQNVKPAGTE
     VAIREAGEVA TPNFIGGAES VGEGVQAVIG GPAAYADQMK TSLSDLRQRM RMPAKLRLEQ
     MIEMDEERVA AVLKQWIHET ASGREADPAK ASAMPELKAA