FLIF_BUCBP
ID FLIF_BUCBP Reviewed; 555 AA.
AC Q89B00;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; OrderedLocusNames=bbp_068;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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 membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Bacterial flagellum basal body {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FliF family. {ECO:0000305}.
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DR EMBL; AE016826; AAO26804.1; -; Genomic_DNA.
DR AlphaFoldDB; Q89B00; -.
DR SMR; Q89B00; -.
DR STRING; 224915.bbp_068; -.
DR EnsemblBacteria; AAO26804; AAO26804; bbp_068.
DR KEGG; bab:bbp_068; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_1_0_6; -.
DR OMA; NYEVNRI; -.
DR Proteomes; UP000000601; 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 3: Inferred from homology;
KW Bacterial flagellum; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..555
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180880"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 555 AA; 63485 MW; 58AF04F7BA88A7BC CRC64;
MNMGRTSNLN VKNRDLKRNF FSNLSLNVRV LLLVFLITLI VFYIFFFKPL NYSILYNNLS
NDDEKSIVSR LISLKIPFKF NQNHSELLIP SNALKKVYLD LAEQGLPKEK KVGFELLDTE
KFGLSQFNEE VNYERALEGE LARSIQKLEN IKTARVHIVL SKSSVFIREK KIPSASVILE
IKPGRYLNYN QINSILHIVA QGVSNLQIEN ITIVDQFGNL LSSMNDLYND SYSNNQLKYS
NEIETGYKNK IESVLVPLVG VNNIHAQVTA QISFDKQENS EERFTPNYSN EKQSVRSVQN
KKNIEFSEKY SDNSFSSNQG VLSNKKLNDL SNSSLLFNHN NIPNFSEQVS STKNSKRNLS
DESVIPQSST NQNYIVNYEL DHVISHNKFN VGNVKRLSVA VVINYVKDKH GKFVSLSTDK
LNSIKKLVCE SVGFSRKRGD SVSVVNFKFS TPEVYFQSPP SNYNKYISFN NLFEFFLICL
GVIILCLLII KLNFLKILFK NKKRIDISNN YAVKDNLTSQ NKGVEDDKEL KKKLSSVLES
DPKEIAMVIR KWISG