ID U3TZZ8_9ENTR Unreviewed; 573 AA.
AC U3TZZ8;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Flagellar M-ring protein {ECO:0000256|ARBA:ARBA00017949, ECO:0000256|PIRNR:PIRNR004862};
GN ORFNames=E05_33580 {ECO:0000313|EMBL:BAN98124.1};
OS Plautia stali symbiont.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=891974 {ECO:0000313|EMBL:BAN98124.1, ECO:0000313|Proteomes:UP000016901};
RN [1] {ECO:0000313|EMBL:BAN98124.1, ECO:0000313|Proteomes:UP000016901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21470838; DOI=10.1016/j.micres.2011.03.001;
RA Kobayashi H., Kawasaki K., Takeishi K., Noda H.;
RT "Symbiont of the stink bug Plautia stali synthesizes rough-type
RT lipopolysaccharide.";
RL Microbiol. Res. 167:48-54(2011).
CC -!- FUNCTION: The M ring may be actively involved in energy transduction.
CC {ECO:0000256|ARBA:ARBA00003820, ECO:0000256|PIRNR:PIRNR004862}.
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.
CC {ECO:0000256|ARBA:ARBA00025936}.
CC -!- SUBCELLULAR LOCATION: Bacterial flagellum basal body
CC {ECO:0000256|ARBA:ARBA00004117, ECO:0000256|PIRNR:PIRNR004862}.
CC Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FliF family. {ECO:0000256|ARBA:ARBA00007971,
CC ECO:0000256|PIRNR:PIRNR004862}.
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DR EMBL; AP012551; BAN98124.1; -; Genomic_DNA.
DR AlphaFoldDB; U3TZZ8; -.
DR KEGG; psts:E05_33580; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_1_0_6; -.
DR Proteomes; UP000016901; Chromosome.
DR GO; GO:0009431; C:bacterial-type flagellum basal body, MS ring; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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 NCBIfam; TIGR00206; fliF; 1.
DR PANTHER; PTHR30046; FLAGELLAR M-RING PROTEIN; 1.
DR PANTHER; PTHR30046:SF0; FLAGELLAR M-RING PROTEIN; 1.
DR Pfam; PF01514; YscJ_FliF; 1.
DR Pfam; PF08345; YscJ_FliF_C; 1.
DR PIRSF; PIRSF004862; FliF; 1.
DR PRINTS; PR01009; FLGMRINGFLIF.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143,
KW ECO:0000256|PIRNR:PIRNR004862};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000313|EMBL:BAN98124.1};
KW Cilium {ECO:0000313|EMBL:BAN98124.1};
KW Flagellum {ECO:0000313|EMBL:BAN98124.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000016901};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..224
FT /note="Flagellar M-ring N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01514"
FT DOMAIN 256..448
FT /note="Flagellar M-ring C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08345"
FT REGION 277..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..374
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 573 AA; 62783 MW; 5E47D3B671F44E2E CRC64;
MNASAAATQD TAKKGFNDLL ARLRANPRIP LIVAAAAAIA VVLALVLWAK APDYRVLYNN
LSDEDGGAIV TQLTQMNIPY QFAENGGALM VPADKEHELS LRLAQQGLPK GGSVGFELMD
KEKFGISQFS EQINYQRALE GELARTIETL GPVKSARVHL AMPKPTLFVR EQKSPSASVT
LNLQPGRALD KGQIQAIQHM VSSSVAGLPL GNVTVVDQAG RLLTRSDSEG RDLNDAQLKY
ASEVEARYQQ RIEAILNPIL DQGNVHAQVT AQINFDRSEQ TDEKYQPNAN PNNTAIRSHQ
TSTNVQNGSP YPGGVPGALS NQPAPANTAP VTNPQQQNNN TANGQQNNNN AQNAGTSTST
AQSSGPSSSS RNDTVNYELD RTIRHTKLNV GDVQRLSVAV VVNYRDDRKG KAVVLNDQQI
KQIEDLTREA MGYSQTRGDS VNVVNSQFNT TEPTGGDLPF WQQQSFFEQL MTAGRWLLVA
LVAFILYRKM VRPQLLRKRE AEKAAAEAAA ARAAAREEEA AYSVQINKDE LDKERKSNNR
MSAEVMSQRI RDMSENDPRV VALVIREWMS NEL
//
