FLIF_BRUME
ID FLIF_BRUME Reviewed; 580 AA.
AC Q8YDM4; Q8YDM3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; OrderedLocusNames=BMEII0151/BMEII0152;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2]
RP FUNCTION IN INFECTION PERSISTENCE, EXPRESSION, AND DISRUPTION PHENOTYPE.
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=15839898; DOI=10.1111/j.1462-5822.2005.00502.x;
RA Fretin D., Fauconnier A., Koehler S., Halling S., Leonard S., Nijskens C.,
RA Ferooz J., Lestrate P., Delrue R.-M., Danese I., Vandenhaute J., Tibor A.,
RA DeBolle X., Letesson J.-J.;
RT "The sheathed flagellum of Brucella melitensis is involved in persistence
RT in a murine model of infection.";
RL Cell. Microbiol. 7:687-698(2005).
CC -!- FUNCTION: The M ring may be actively involved in energy transduction
CC (By similarity). The flagellum is required to cause a persistent
CC disease in a murine model of infection. {ECO:0000250,
CC ECO:0000269|PubMed:15839898}.
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 -!- INDUCTION: Transiently expressed during the early exponential phase.
CC -!- DISRUPTION PHENOTYPE: A fliF mutant is attenuated in a murine model of
CC infection. As the infection progresses, the number of cfu per spleen
CC from mice infected with the mutant is significantly lower than the
CC number from mice infected with the wild-type.
CC {ECO:0000269|PubMed:15839898}.
CC -!- MISCELLANEOUS: Induced at 24 and 48 hours post infection in HeLa cells.
CC -!- SIMILARITY: Belongs to the FliF family. {ECO:0000305}.
CC -!- CAUTION: Despite the presence of a stop codon in position 243 in the
CC fliF gene and in position 127 in the flhA gene, it has been shown that
CC B.melitensis is able to express genes corresponding to the M ring, the
CC hook and the filament of the flagellar apparatus in the early log phase
CC of growth in 2YT broth. Under these conditions, a polar and sheathed
CC flagellar structure is visible by transmission electron microscopy.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL53393.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE008918; AAL53392.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AE008918; AAL53393.1; ALT_SEQ; Genomic_DNA.
DR PIR; AE3528; AE3528.
DR PIR; AF3528; AF3528.
DR AlphaFoldDB; Q8YDM4; -.
DR SMR; Q8YDM4; -.
DR STRING; 224914.BMEII0152; -.
DR EnsemblBacteria; AAL53392; AAL53392; BMEII0151.
DR EnsemblBacteria; AAL53393; AAL53393; BMEII0152.
DR KEGG; bme:BMEII0151; -.
DR KEGG; bme:BMEII0152; -.
DR eggNOG; COG1766; Bacteria.
DR OMA; ITTRPHY; -.
DR PRO; PR:Q8YDM4; -.
DR Proteomes; UP000000419; 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 1: Evidence at protein level;
KW Bacterial flagellum; Cell inner membrane; Cell membrane; Membrane;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..580
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180876"
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..339
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; 62161 MW; 3451EB2C2F3C1456 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 ELTNYEVNSM TVSTVSDGYS
IKRLSIAVVI DQARLLQTAG TTPPPANFVD QQITKIRDLV ATAAGLNTNR GDVINVTAVN
FLDSAGADME PVSAPWTDTL LRQSGSYANA LAILAAVGLL IWFGLRPLLR DQNVKPAGTE
VAIREAGEVA TPNFIGGAES VGEGVQAVIG GPAAYADQMK TSLSDLRQRM RMPAKLRLEQ
MIEMDEERVA AVLKQWIHET ASGREADPAK ASAMPELKAA
