FLIF_BORBU
ID FLIF_BORBU Reviewed; 569 AA.
AC Q44912; Q57338;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; OrderedLocusNames=BB_0291;
OS Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)
OS (Borrelia burgdorferi).
OC Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX NCBI_TaxID=224326;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RA Dunn J.J., Butler-Loffredo L., Kieleczawa J., Medalle J., Luft B.J.;
RL Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9079915; DOI=10.1128/jb.179.7.2289-2299.1997;
RA Ge Y., Old I.G., Saint Girons I., Charon N.W.;
RT "Molecular characterization of a large Borrelia burgdorferi motility operon
RT which is initiated by a consensus sigma70 promoter.";
RL J. Bacteriol. 179:2289-2299(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=212;
RA Ge Y., Saint-Girons I., Old I.G., Yelton D.B., Charon N.W.;
RT "Identification of a major motility operon in B. burgdorferi.";
RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35210 / DSM 4680 / CIP 102532 / B31;
RX PubMed=9403685; DOI=10.1038/37551;
RA Fraser C.M., Casjens S., Huang W.M., Sutton G.G., Clayton R.A.,
RA Lathigra R., White O., Ketchum K.A., Dodson R.J., Hickey E.K., Gwinn M.L.,
RA Dougherty B.A., Tomb J.-F., Fleischmann R.D., Richardson D.L.,
RA Peterson J.D., Kerlavage A.R., Quackenbush J., Salzberg S.L., Hanson M.,
RA van Vugt R., Palmer N., Adams M.D., Gocayne J.D., Weidman J.F.,
RA Utterback T.R., Watthey L., McDonald L.A., Artiach P., Bowman C.,
RA Garland S.A., Fujii C., Cotton M.D., Horst K., Roberts K.M., Hatch B.,
RA Smith H.O., Venter J.C.;
RT "Genomic sequence of a Lyme disease spirochaete, Borrelia burgdorferi.";
RL Nature 390:580-586(1997).
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 -!- SEQUENCE CAUTION:
CC Sequence=AAA87352.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U43739; AAA85614.1; -; Genomic_DNA.
DR EMBL; L76303; AAB51410.1; -; Genomic_DNA.
DR EMBL; L40501; AAA87352.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE000783; AAC66657.1; -; Genomic_DNA.
DR PIR; C70136; C70136.
DR RefSeq; NP_212425.1; NC_001318.1.
DR RefSeq; WP_002556890.1; NC_001318.1.
DR AlphaFoldDB; Q44912; -.
DR SMR; Q44912; -.
DR STRING; 224326.BB_0291; -.
DR PRIDE; Q44912; -.
DR EnsemblBacteria; AAC66657; AAC66657; BB_0291.
DR GeneID; 56567722; -.
DR KEGG; bbu:BB_0291; -.
DR PATRIC; fig|224326.49.peg.690; -.
DR HOGENOM; CLU_028108_2_0_12; -.
DR OMA; NYEVNRI; -.
DR Proteomes; UP000001807; 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 PRINTS; PR01009; FLGMRINGFLIF.
DR TIGRFAMs; TIGR00206; fliF; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..569
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180874"
FT TRANSMEM 25..45
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 473..493
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 281..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..326
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 184..187
FT /note="GSDI -> LVLIF (in Ref. 3; AAA87352)"
FT /evidence="ECO:0000305"
FT CONFLICT 203..208
FT /note="YAIEGL -> PICHEGF (in Ref. 3; AAA87352)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 569 AA; 65133 MW; 840AB3D57C141AB1 CRC64;
MSKFFTNFFV SAKGIFKKAS TVQKIALGLI IFFVILALVF LIGFSTKSQS IALFGVEIKD
QYLLDRISQR LDRENVKYFL SSDGRIYLDD EKLAKKMRAI LVREELVPVH MDPWALFDID
RWTITDFERS INLRRSITRA VEQHIVALDD VDAVSVNLVM PEKALFKESQ EPVKASVRIT
PRPGSDIITN RKKVEGLVKL IQYAIEGLES DNIAIVDNSG TILNDFSNLD GIDRIDLAEK
ERKLKLKYEA MLRGEIDSAL SKVLSVDRFM IARVNVKLDT SKETTESKEY APIELQSQDP
KASYNTRKVS DSTIISSQTQ KKEYQGQGYS PWGPPGQEGN TPPEYQDLSD ITGKYNESQE
IKNVALNEKK STSEKEPARI VGVSLGIFVD GIWNFVYDEK GDFVIENGMR KREYKPMALE
EIKNIEDVLQ SSFEYKPERG DSITVRNISF DRMNEFREID ENYFASERFK YFLFIASIVF
SLLILVFTIF FAISRELERR RRLREEELAK QAHLRRQQAL MDGGDDIGVD DVVGGIREGD
ELQSNAELLA REKPEDVAKL IRTWLLKNA
