LPTB_ACIFI
ID LPTB_ACIFI Reviewed; 241 AA.
AC P24693;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB;
DE EC=7.5.2.-;
GN Name=lptB;
OS Acidithiobacillus ferridurans.
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1232575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX PubMed=2198257; DOI=10.1128/jb.172.8.4399-4406.1990;
RA Berger D.K., Woods D.R., Rawlings D.E.;
RT "Complementation of Escherichia coli sigma 54 (NtrA)-dependent formate
RT hydrogenlyase activity by a cloned Thiobacillus ferrooxidans ntrA gene.";
RL J. Bacteriol. 172:4399-4406(1990).
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. Probably responsible for energy coupling to the
CC transport system (By similarity). {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: Cytoplasm. Cell inner membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}; Cytoplasmic side
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Outer membrane
CC lipopolysaccharide export (TC 1.B.42) family. {ECO:0000305}.
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DR EMBL; M58480; AAA27378.1; -; Genomic_DNA.
DR PIR; A37761; A37761.
DR RefSeq; WP_012537553.1; NZ_QKQP01000005.1.
DR AlphaFoldDB; P24693; -.
DR SMR; P24693; -.
DR STRING; 380394.Lferr_2634; -.
DR OMA; LPMYQRA; -.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd03218; ABC_YhbG; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR030921; LPS_export_LptB.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR04406; LPS_export_lptB; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Cytoplasm; Membrane;
KW Nucleotide-binding; Translocase; Transport.
FT CHAIN 1..241
FT /note="Lipopolysaccharide export system ATP-binding protein
FT LptB"
FT /id="PRO_0000093186"
FT DOMAIN 5..237
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 37..44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 241 AA; 27023 MW; 46535C464C78EF72 CRC64;
MSELLQAQSL FKSYRRRVVV RDVSVQVATG EVVGLLGPNG AGKTTTFYMM VGLVRPDRGH
IFLQQRDITA LPMHERARMG LGYLPQEPSV FRQMSAADNV LAVLETLPLS PVERQERQEQ
LLSELHLHAL RDTKGHSLSG GERRRVEIAR ALAMSPRFIL LDEPFAGIDP ISVLEIQRLI
RDLRARGIGV LITDHNVRET LGICERAYIL HDGKVLTAGS PQEIVDDPMV RQVYLGDQFQ
I
