ID A5IJ88_THEP1 Unreviewed; 249 AA.
AC A5IJ88;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=Flagellar biosynthetic protein FliP {ECO:0000256|ARBA:ARBA00021714, ECO:0000256|RuleBase:RU362069};
GN Name=fliP {ECO:0000256|RuleBase:RU362069};
GN OrderedLocusNames=Tpet_0232 {ECO:0000313|EMBL:ABQ46261.1};
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Thermotoga.
OX NCBI_TaxID=390874 {ECO:0000313|EMBL:ABQ46261.1, ECO:0000313|Proteomes:UP000006558};
RN [1] {ECO:0000313|Proteomes:UP000006558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC {ECO:0000313|Proteomes:UP000006558};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABQ46261.1, ECO:0000313|Proteomes:UP000006558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1
RC {ECO:0000313|Proteomes:UP000006558};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
CC -!- FUNCTION: Plays a role in the flagellum-specific transport system.
CC {ECO:0000256|RuleBase:RU362069}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362069};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362069}. Bacterial
CC flagellum basal body {ECO:0000256|RuleBase:RU362069}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FliP/MopC/SpaP family.
CC {ECO:0000256|ARBA:ARBA00006257, ECO:0000256|RuleBase:RU362069}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000702; ABQ46261.1; -; Genomic_DNA.
DR RefSeq; WP_011942906.1; NC_009486.1.
DR AlphaFoldDB; A5IJ88; -.
DR STRING; 390874.Tpet_0232; -.
DR KEGG; tpt:Tpet_0232; -.
DR eggNOG; COG1338; Bacteria.
DR HOGENOM; CLU_042028_0_1_0; -.
DR Proteomes; UP000006558; Chromosome.
DR GO; GO:0009425; C:bacterial-type flagellum basal body; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0044781; P:bacterial-type flagellum organization; IEA:UniProtKB-UniRule.
DR GO; GO:0009306; P:protein secretion; IEA:UniProtKB-UniRule.
DR InterPro; IPR005837; FliP.
DR InterPro; IPR005838; T3SS_IM_P.
DR NCBIfam; TIGR01103; fliP; 1.
DR PANTHER; PTHR30587; FLAGELLAR BIOSYNTHETIC PROTEIN FLIP; 1.
DR PANTHER; PTHR30587:SF0; FLAGELLAR BIOSYNTHETIC PROTEIN FLIP; 1.
DR Pfam; PF00813; FliP; 1.
DR PRINTS; PR00951; FLGBIOSNFLIP.
DR PRINTS; PR01302; TYPE3IMPPROT.
DR PROSITE; PS01061; FLIP_2; 1.
PE 3: Inferred from homology;
KW Bacterial flagellum {ECO:0000256|ARBA:ARBA00023143};
KW Bacterial flagellum biogenesis {ECO:0000256|ARBA:ARBA00022795,
KW ECO:0000256|RuleBase:RU362069};
KW Bacterial flagellum protein export {ECO:0000256|ARBA:ARBA00023225,
KW ECO:0000256|RuleBase:RU362069};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU362069};
KW Cell projection {ECO:0000313|EMBL:ABQ46261.1};
KW Cilium {ECO:0000313|EMBL:ABQ46261.1};
KW Flagellum {ECO:0000313|EMBL:ABQ46261.1};
KW Hydrolase {ECO:0000313|EMBL:ABQ46261.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362069};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU362069};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362069};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362069};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362069}.
FT TRANSMEM 45..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362069"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362069"
FT TRANSMEM 191..215
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362069"
FT TRANSMEM 227..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362069"
SQ SEQUENCE 249 AA; 28180 MW; C5C7F239AAE07E59 CRC64;
MRKLLLILLI FLPLLYFSQE IPFPSISIGV RPAEEPEDLV VTLEILLVLT VLALAPSILV
LFTSFTRIIV VFSLFRNALG TRQTPPNQVM IGLALFLTFL IMQPVWNDIY NNAITPYLNK
EIGYQEMFQR VNTRIREFMI NELKNHHNED NVFMLAKNSG IEIAKIEEAP NAVLIPAFVL
GELEVAFKMG VVLYVPFIVI DMIVASILLA MGMIMIPPVF VSLPFKILIF VMANGWDLLV
EGLIKSFAR
//