ID K0BZR2_CYCSP Unreviewed; 378 AA.
AC K0BZR2;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Lipopolysaccharide export system permease protein LptF {ECO:0000256|ARBA:ARBA00014213};
GN OrderedLocusNames=Q91_0399 {ECO:0000313|EMBL:AFT66439.1};
OS Cycloclasticus sp. (strain P1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=385025 {ECO:0000313|EMBL:AFT66439.1, ECO:0000313|Proteomes:UP000006282};
RN [1] {ECO:0000313|EMBL:AFT66439.1, ECO:0000313|Proteomes:UP000006282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1 {ECO:0000313|EMBL:AFT66439.1,
RC ECO:0000313|Proteomes:UP000006282};
RX PubMed=23144416; DOI=10.1128/JB.01837-12;
RA Lai Q., Li W., Wang B., Yu Z., Shao Z.;
RT "Complete genome sequence of the pyrene-degrading bacterium Cycloclasticus
RT sp. strain P1.";
RL J. Bacteriol. 194:6677-6677(2012).
CC -!- FUNCTION: Part of the ABC transporter complex LptBFG involved in the
CC translocation of lipopolysaccharide (LPS) from the inner membrane to
CC the outer membrane. {ECO:0000256|ARBA:ARBA00002265}.
CC -!- SUBUNIT: Component of the lipopolysaccharide transport and assembly
CC complex. The LptBFG transporter is composed of two ATP-binding proteins
CC (LptB) and two transmembrane proteins (LptF and LptG).
CC {ECO:0000256|ARBA:ARBA00026081}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the LptF/LptG family.
CC {ECO:0000256|ARBA:ARBA00007725}.
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DR EMBL; CP003230; AFT66439.1; -; Genomic_DNA.
DR AlphaFoldDB; K0BZR2; -.
DR STRING; 385025.Q91_0399; -.
DR KEGG; cyq:Q91_0399; -.
DR PATRIC; fig|385025.3.peg.410; -.
DR HOGENOM; CLU_028799_0_2_6; -.
DR Proteomes; UP000006282; 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; IPR030922; LptF.
DR InterPro; IPR005495; LptG/LptF_permease.
DR NCBIfam; TIGR04407; LptF_YjgP; 1.
DR PANTHER; PTHR33529:SF7; LIPOPOLYSACCHARIDE EXPORT SYSTEM PERMEASE PROTEIN LPTF; 1.
DR PANTHER; PTHR33529; SLR0882 PROTEIN-RELATED; 1.
DR Pfam; PF03739; LptF_LptG; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006282};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 347..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 378 AA; 42278 MW; ED7F1E2BEF3EE532 CRC64;
MPNYKPNTLL MSAFKLKIID RLLVTQISKM MLGVMTVLTV ILLSQRLVRL FSKVTAGELS
ADVVLSLVGF NLLLLMIKIL PVALLLSILL VLGRMYRDHE MTALFSSGIG LTQIYRGIFI
FVVPLFALTI YLSLVTAPTL MQAIERVKTS DQANLDIRGI TDGRFNEYSR GDLVFYVEKI
TSDDKMLNVF IQNRQHGKLG ITSSKSGEIK VDPVTGDRFI ILKDGNRYEG VPGQADYKIT
NFKEYGVVVA EKSSAQVSFG TKETSTIQLM AMKSPRAISE LQKRWSVPLA LITFALLAVP
ISRVSPRAGM YGNLLTALLI YIVFENFMSL SHSWLVKGVT APWFGIWWVH LLLIGVTAIM
VVNMHGVSYV KKKVMFKR
//
