ID B1LHP3_ECOSM Unreviewed; 548 AA.
AC B1LHP3;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Flagellar M-ring protein {ECO:0000256|ARBA:ARBA00017949, ECO:0000256|PIRNR:PIRNR004862};
GN Name=lfiF {ECO:0000313|EMBL:ACB18368.1};
GN OrderedLocusNames=EcSMS35_0250 {ECO:0000313|EMBL:ACB18368.1};
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB18368.1, ECO:0000313|Proteomes:UP000007011};
RN [1] {ECO:0000313|EMBL:ACB18368.1, ECO:0000313|Proteomes:UP000007011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(2008).
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; CP000970; ACB18368.1; -; Genomic_DNA.
DR RefSeq; WP_000993677.1; NC_010498.1.
DR AlphaFoldDB; B1LHP3; -.
DR KEGG; ecm:EcSMS35_0250; -.
DR HOGENOM; CLU_028108_1_1_6; -.
DR Proteomes; UP000007011; 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:ACB18368.1};
KW Cilium {ECO:0000313|EMBL:ACB18368.1};
KW Flagellum {ECO:0000313|EMBL:ACB18368.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 437..458
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 259..418
FT /note="Flagellar M-ring C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08345"
FT REGION 294..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 59919 MW; 623AA77A40287E4B CRC64;
MNAQIKKLTQ AFPAFRLRLA DNKRWALMAG VGLAVAATAI IVSVLWTGNR GYVSLYGRQE
NLPVSQIVTV LDGEKLSYRI DPQSGQILVP EDELSKTRMT LAAKGVQAIL PSGYELMDKD
EVLGSSQFVQ NVRYKRSLEG ELAQSIMSLD AVESARVHLA LNEESSFVVS DEPQNSASVV
VRLHYGAKLN MDQVNAIVHL VSGSIPGLHA SKVSVVDQAG NLLTDGIGAG EAVSAATRKR
DQILKDIQDK TRASVANVLD SLVGSGNYRV SVMPDLDLSN IDETQEHYGD APKINREENV
LDSDTNQVAM GVPGSLSNRP PIAANQMTNG TEENRSPEAL SKHSESKRDY SYDRSVQHIQ
HPGFAVKRLN VAVVLNQNAP ALKNWKPEQT TQLTALLNNA AGIDVQRGDN LTLSLLNFVP
QAVPVEPIIP LWKDDSVLAW VRLIGCGLLA LLLLFFVVRP VMKRLTAVRA PVITPEPEAV
SEPWIAMPEE ERKNVDLPSL PGDDSLPSQS SGLEVKLEFL QKLAMSDTDR VAEVLRQWIT
SNERIDNK
//
