LPTF_SHIFL
ID LPTF_SHIFL Reviewed; 366 AA.
AC P0AFA1; P39340;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Lipopolysaccharide export system permease protein LptF;
GN Name=lptF; OrderedLocusNames=SF4228, S4489;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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:0000250}.
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) (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the LptF/LptG family. {ECO:0000305}.
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DR EMBL; AE005674; AAN45647.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP19435.1; -; Genomic_DNA.
DR RefSeq; NP_709940.2; NC_004337.2.
DR RefSeq; WP_000584114.1; NZ_UIQL01000085.1.
DR PDB; 6S8G; EM; 3.50 A; F=1-366.
DR PDB; 6S8H; EM; 3.70 A; F=1-366.
DR PDB; 6S8N; EM; 3.10 A; F=1-366.
DR PDBsum; 6S8G; -.
DR PDBsum; 6S8H; -.
DR PDBsum; 6S8N; -.
DR AlphaFoldDB; P0AFA1; -.
DR SMR; P0AFA1; -.
DR STRING; 198214.SF4228; -.
DR EnsemblBacteria; AAN45647; AAN45647; SF4228.
DR EnsemblBacteria; AAP19435; AAP19435; S4489.
DR GeneID; 1027392; -.
DR GeneID; 66671820; -.
DR KEGG; sfl:SF4228; -.
DR KEGG; sfx:S4489; -.
DR PATRIC; fig|198214.7.peg.4987; -.
DR HOGENOM; CLU_028799_0_2_6; -.
DR OMA; ELQWRIA; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 PANTHER; PTHR33529; PTHR33529; 1.
DR Pfam; PF03739; LptF_LptG; 1.
DR TIGRFAMs; TIGR04407; LptF_YjgP; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..366
FT /note="Lipopolysaccharide export system permease protein
FT LptF"
FT /id="PRO_0000169774"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 37..53
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 75..100
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 122..269
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..316
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 317..327
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 3..36
FT /evidence="ECO:0007829|PDB:6S8N"
FT TURN 37..41
FT /evidence="ECO:0007829|PDB:6S8N"
FT STRAND 44..47
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 56..81
FT /evidence="ECO:0007829|PDB:6S8N"
FT TURN 82..85
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 86..91
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:6S8N"
FT TURN 110..115
FT /evidence="ECO:0007829|PDB:6S8N"
FT STRAND 116..122
FT /evidence="ECO:0007829|PDB:6S8N"
FT TURN 123..132
FT /evidence="ECO:0007829|PDB:6S8N"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 267..281
FT /evidence="ECO:0007829|PDB:6S8N"
FT STRAND 282..286
FT /evidence="ECO:0007829|PDB:6S8N"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 297..299
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 300..317
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 319..322
FT /evidence="ECO:0007829|PDB:6S8N"
FT HELIX 329..346
FT /evidence="ECO:0007829|PDB:6S8N"
FT STRAND 349..351
FT /evidence="ECO:0007829|PDB:6S8N"
SQ SEQUENCE 366 AA; 40358 MW; 69A564AA22CBFFEA CRC64;
MIIIRYLVRE TLKSQLAILF ILLLIFFCQK LVRILGAAVD GDIPANLVLS LLGLGVPEMA
QLILPLSLFL GLLMTLGKLY TESEITVMHA CGLSKAVLVK AAMILAVFTA IVAAVNVMWA
GPWSSRHQDE VLAEAKANPG MAALAQGQFQ QATNGSSVLF IESVDGSDFK DVFLAQIRPK
GNARPSVVVA DSGHLTQLRD GSQVVTLNQG TRFEGTALLR DFRITDFQDY QAIIGHQAVA
LDPNDTDQMD MRTLWNTDTD RARAELNWRI TLVFTVFMMA LMVVPLSVVN PRQGRVLSML
PAMLLYLLFF LIQTSLKSNG GKGKLDPTLW MWTVNLIYLA LAIVLNLWDT VPVRRLRASF
SRKGAV
