ID U5MZ43_CLOSA Unreviewed; 524 AA.
AC U5MZ43;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Flagellar M-ring protein {ECO:0000256|PIRNR:PIRNR004862};
GN Name=fliF {ECO:0000313|EMBL:AGX44896.1};
GN ORFNames=CLSA_c39360 {ECO:0000313|EMBL:AGX44896.1};
OS Clostridium saccharobutylicum DSM 13864.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX44896.1, ECO:0000313|Proteomes:UP000017118};
RN [1] {ECO:0000313|EMBL:AGX44896.1, ECO:0000313|Proteomes:UP000017118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX44896.1};
RX PubMed=24285650;
RA Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA Gottschalk G., Daniel R.;
RT "Complete Genome Sequence of the Solvent Producer Clostridium
RT saccharobutylicum NCP262 (DSM 13864).";
RL Genome Announc. 1:e00997-13(2013).
CC -!- FUNCTION: The M ring may be actively involved in energy transduction.
CC {ECO:0000256|PIRNR:PIRNR004862}.
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; CP006721; AGX44896.1; -; Genomic_DNA.
DR RefSeq; WP_022749179.1; NZ_AYXL01000271.1.
DR AlphaFoldDB; U5MZ43; -.
DR GeneID; 55476234; -.
DR KEGG; csb:CLSA_c39360; -.
DR PATRIC; fig|1345695.10.peg.2764; -.
DR eggNOG; COG1766; Bacteria.
DR HOGENOM; CLU_028108_2_0_9; -.
DR OrthoDB; 9807026at2; -.
DR Proteomes; UP000017118; 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 CDD; cd12087; TM_EGFR-like; 1.
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:AGX44896.1};
KW Cilium {ECO:0000313|EMBL:AGX44896.1};
KW Flagellum {ECO:0000313|EMBL:AGX44896.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017118};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 432..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 45..217
FT /note="Flagellar M-ring N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01514"
FT DOMAIN 255..405
FT /note="Flagellar M-ring C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08345"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 524 AA; 57614 MW; 4D0174D5B478123D CRC64;
MNRLLEKVKG FWEKFKSQSK KIKIAVVISI IAIIAAIASA IIYSSSNKYE ILFSNLDPND
TQTIVKSLND DKVQTKIDGN TIYVPSNKVD ELRLKYAPNL TAGGSKGYEL MDSGSSFGMT
DEEFKIKKVR MEEGELEKTI KSFPQIQEAR VHITESQDSV FVKEKTPGSA AVYLKIKQGN
SINEDQVKSI VALVSGATEK IPKENIQVID DKMNLLTKDI NSDETDPVNS EALTKQQDAE
KKYEDKLQKA IVSLLEPTIG QGKVKATVNV NLDFDSKQKT QTVVDPNKVI VSQENSKESN
TSAGGSTTSQ SPVDNNMSNQ ITSANTNNGN NSTSAKEDQK TNYDTGKTES KVISAPGEVK
RLTASVIVDG QVDAATQATL ENIVKNAIGL DANRGDQVTV AGMTFDTSSQ DAAKAQIDAM
NAQEAASSKN KMMIIGGILG AILLGTIAFF IIKRRKKKQE EEDQLLDTLV DDTIIPKEPE
EFDPIEFEVK TKNSHLENEI KKYATEKPEQ VVEIIKSWLT EDER
//
