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Database: UniProt
Entry: Q66BR7_YERPS
LinkDB: Q66BR7_YERPS
Original site: Q66BR7_YERPS 
ID   Q66BR7_YERPS            Unreviewed;       570 AA.
AC   Q66BR7;
DT   11-OCT-2004, integrated into UniProtKB/TrEMBL.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Flagellar M-ring protein {ECO:0000256|ARBA:ARBA00017949, ECO:0000256|PIRNR:PIRNR004862};
DE   Flags: Precursor;
GN   Name=fliF {ECO:0000313|EMBL:CAH20942.1};
GN   OrderedLocusNames=YPTB1703 {ECO:0000313|EMBL:CAH20942.1};
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123 {ECO:0000313|EMBL:CAH20942.1, ECO:0000313|Proteomes:UP000001011};
RN   [1] {ECO:0000313|EMBL:CAH20942.1, ECO:0000313|Proteomes:UP000001011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953 {ECO:0000313|Proteomes:UP000001011};
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH20942.1; -; Genomic_DNA.
DR   RefSeq; WP_011192181.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66BR7; -.
DR   GeneID; 66841863; -.
DR   KEGG; ypo:BZ17_797; -.
DR   KEGG; yps:YPTB1703; -.
DR   PATRIC; fig|273123.14.peg.845; -.
DR   Proteomes; UP000001011; 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:CAH20942.1};
KW   Cilium {ECO:0000313|EMBL:CAH20942.1};
KW   Flagellum {ECO:0000313|EMBL:CAH20942.1};
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        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..223
FT                   /note="Flagellar M-ring N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01514"
FT   DOMAIN          255..447
FT                   /note="Flagellar M-ring C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08345"
FT   REGION          276..329
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          355..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        285..309
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        355..372
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   570 AA;  61624 MW;  D8F241170A9CF6B0 CRC64;
     MNASITGGEN RENTFTMTLA RLRANPKIPL LIAAAAAIAI IVALMLWAKS PDYRVLYSNL
     SDRDGGDIVT QLTQLNIPYR FADNGGALLI PAEKVHETRL RLAQQGLPKG GAVGFELLDQ
     EKFGISQFSE QINYQRALEG ELSRTIGTLG PVLNVRVHLA MPKPSLFVRE QKSPTASVTL
     ALQPGRALDD GQINAIVYMV SSSVAGLPPG NVTVVDQTGR LLTQSDSAGR DLNASQLKFT
     SEVENRYQRR IENILAPMVG NGNVHAQVTA QVDFASREQT DEEYKPNQAA NQGAVRSQQV
     STSEQLGGTN VGGVPGALSN QPPVAPIAPI EIPQPAGAAA NNAAPANAAT TANANTTATA
     AKASSSNSRH DQTTNFEVDR TIRHTQQQAG MVQRLSVAVV VNYTSDKAGK PIALSKDQLA
     QVESLTREAM GFSTVRGDTL NVVNTPFTAS DDTRGSSLPF WQQQSFFDQL LNAGRYLLIL
     LVAWILWRKL LRPMLAKKQV ADKAAASVNN IVQTAQAAET VKQSKEELAL RKKNQQRVSA
     EVQAQRIREL ADKDPRVVAL VIRQWMSNDQ
//
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