FLIF_BUCAP
ID FLIF_BUCAP Reviewed; 556 AA.
AC Q8KA45;
DT 08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Flagellar M-ring protein;
GN Name=fliF; OrderedLocusNames=BUsg_067;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; AE013218; AAM67637.1; -; Genomic_DNA.
DR RefSeq; WP_011053603.1; NC_004061.1.
DR AlphaFoldDB; Q8KA45; -.
DR SMR; Q8KA45; -.
DR STRING; 198804.BUsg_067; -.
DR EnsemblBacteria; AAM67637; AAM67637; BUsg_067.
DR KEGG; bas:BUsg_067; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_1_0_6; -.
DR OMA; NYEVNRI; -.
DR OrthoDB; 167675at2; -.
DR Proteomes; UP000000416; 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; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..556
FT /note="Flagellar M-ring protein"
FT /id="PRO_0000180879"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 459..479
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 298..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 556 AA; 64260 MW; 57BB4D66475FE8F3 CRC64;
MNFSTIEESV SEEKKKFNNF LSYFFKNSRV LIILFVLAVI TTVSISMWRK SPDYQVLYNN
LSNEDGEMII DQLNQMQIPY KLSEDSGQLL VPKDKVYELR LHFSENNSPH RDIGYEILDK
ERFGVSQFGE QINYQRALEG ELARTIEKIN VVKNAKIHIA FPKNSLFLED KKKPSVSVIL
NLKSNQGLDH SQVNAILHLI SSSICDLSIE NITIIDQFGK LLNNSSLGLN QIDDLKLRYS
EEVESRYRNR IKNILEPLLG FNNVYAQVTA QINFNSHEKT QEKYTPNTNY KNQAIRSRQS
TVNDKINNRK EENKPDELFP QTSFSSNKDL NSTTYSNKKI KKSIIQNNQD NNILHSNSAI
SHDDTINYEL NHSLSHTKMN IGEIKRLSAA VIVNFVKDKN GKSVPINVEQ IKKIKNLVRE
AIGYSKVRGD SVYVVNESFF QKNKNSPIKL LKDSNQSNFY STFLTFTPWF ISLFFLFFLV
KKCFFSSSKN NINNQSYKNK TEEDLLEKDT KAENISELKF SKTSNTDKLI HQICNISNQN
PRIIASIIRQ WMSDKK