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Database: UniProt
Entry: I3TLP9_TISMK
LinkDB: I3TLP9_TISMK
Original site: I3TLP9_TISMK 
ID   I3TLP9_TISMK            Unreviewed;       384 AA.
AC   I3TLP9;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Putative permease {ECO:0000313|EMBL:AFK53687.1};
GN   OrderedLocusNames=TMO_1848 {ECO:0000313|EMBL:AFK53687.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK53687.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK53687.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK53687.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP003236; AFK53687.1; -; Genomic_DNA.
DR   RefSeq; WP_014745365.1; NC_017956.1.
DR   AlphaFoldDB; I3TLP9; -.
DR   STRING; 1110502.TMO_1848; -.
DR   KEGG; tmo:TMO_1848; -.
DR   PATRIC; fig|1110502.3.peg.1906; -.
DR   eggNOG; COG0795; Bacteria.
DR   HOGENOM; CLU_028799_2_0_5; -.
DR   Proteomes; UP000005258; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR030923; LptG.
DR   InterPro; IPR005495; LptG/LptF_permease.
DR   NCBIfam; TIGR04408; LptG_lptG; 1.
DR   PANTHER; PTHR33529:SF2; LIPOPOLYSACCHARIDE EXPORT SYSTEM PERMEASE PROTEIN LPTG; 1.
DR   PANTHER; PTHR33529; SLR0882 PROTEIN-RELATED; 1.
DR   Pfam; PF03739; LptF_LptG; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        36..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        329..351
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        357..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  41095 MW;  05FA0C27AEFEF3FA CRC64;
     MTQPSSSAGH VRAGRAPSTP RRHVSTTLSL YLARHMLNSV GLVLAVVMGL VLVVDLIELL
     RRAAGDDVPV ATLIGMAILK NPFQLQKIAP FAVLIGGMIT FSRLTRTNEL VVARAAGVSV
     WQFMAPPVGV ALLLGAFLVA VFNPLAAMMA SRYESLDARY IGGRSSLLSV GPGGLWLRER
     LDGAPVVIHA TRMAAAGTDL GNVTIFRYGP DETFRDRIDA ARATLGNQVW HIENAVISAP
     DRMSERAETM EQATQMTREQ ILDSFANPET MSFWALPGFI AQLRDAGFSA LQHRLYWHSV
     LALPLLMTAM VIISATFGLR FTRRGGAGIT IAGGVFTGFL LYFLTGVVYA LGQSGGLPVV
     LAAWTPAGVA ALFGIATLLH LEDG
//
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