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Database: UniProt
Entry: A5IJ88_THEP1
LinkDB: A5IJ88_THEP1
Original site: A5IJ88_THEP1 
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}.
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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
//
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