FLIP_CERSP
ID FLIP_CERSP Reviewed; 301 AA.
AC O85133;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Flagellar biosynthetic protein FliP;
GN Name=fliP;
OS Cereibacter sphaeroides (Rhodobacter sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=1063;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=WS8;
RX PubMed=9683497; DOI=10.1128/jb.180.15.3978-3982.1998;
RA Garcia N., Campos A., Osorio A., Poggio S., Gonzalez-Pedrajo B.,
RA Camarena L., Dreyfus G.;
RT "The flagellar switch genes fliM and fliN of Rhodobacter sphaeroides are
RT contained in a large flagellar gene cluster.";
RL J. Bacteriol. 180:3978-3982(1998).
CC -!- FUNCTION: Plays a role in the flagellum-specific transport system.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Bacterial flagellum basal body {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FliP/MopC/SpaP family. {ECO:0000305}.
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DR EMBL; AF044580; AAC32322.1; -; Genomic_DNA.
DR AlphaFoldDB; O85133; -.
DR SMR; O85133; -.
DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
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:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR InterPro; IPR005837; FliP.
DR InterPro; IPR005838; T3SS_IM_P.
DR PANTHER; PTHR30587; PTHR30587; 1.
DR PANTHER; PTHR30587:SF0; PTHR30587:SF0; 1.
DR Pfam; PF00813; FliP; 1.
DR PRINTS; PR00951; FLGBIOSNFLIP.
DR PRINTS; PR01302; TYPE3IMPPROT.
DR TIGRFAMs; TIGR01103; fliP; 1.
DR PROSITE; PS01060; FLIP_1; 1.
DR PROSITE; PS01061; FLIP_2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum; Bacterial flagellum biogenesis;
KW Bacterial flagellum protein export; Cell membrane; Membrane;
KW Protein transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..301
FT /note="Flagellar biosynthetic protein FliP"
FT /id="PRO_0000191988"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 301 AA; 32145 MW; 2F7960C9C7CC0061 CRC64;
MTRRNPMRRE MPSPACPGHR HAPPRQAIET GARQMRAAPC RPNRPGKARA PRAARMMALA
GSALAAGLLL AGSAAAAGFP AISVTEGTGG TSYLLSLQIL ALMTALTVLP SLVLGMSAFT
RIIIVLSILR QALGTQQTPP NQVLIALALF LTFFVMQPTL GALYEQSLSP FLDGQIEAQP
AIERGGAIMK DFLIANTRQN DLLMFSDLAG AGPYAEPTEV PFSTLLPAFM TSELKTAFQI
GFLLFLPFLV IDMVIASILM ALGMMMLSPM LVSLPFKLLL FVLVDGWALT VGSLAASYWG
Q