ID A0A254TI69_9BURK Unreviewed; 246 AA.
AC A0A254TI69;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB {ECO:0000256|ARBA:ARBA00017803};
GN ORFNames=AYR66_25420 {ECO:0000313|EMBL:OWW22336.1};
OS Noviherbaspirillum denitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=1968433 {ECO:0000313|EMBL:OWW22336.1, ECO:0000313|Proteomes:UP000197535};
RN [1] {ECO:0000313|EMBL:OWW22336.1, ECO:0000313|Proteomes:UP000197535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSA40 {ECO:0000313|EMBL:OWW22336.1,
RC ECO:0000313|Proteomes:UP000197535};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00024818}.
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:ARBA00004515}; Peripheral membrane protein
CC {ECO:0000256|ARBA:ARBA00004515}; Cytoplasmic side
CC {ECO:0000256|ARBA:ARBA00004515}. Cytoplasm
CC {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Outer membrane
CC lipopolysaccharide export (TC 1.B.42) family.
CC {ECO:0000256|ARBA:ARBA00010865}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OWW22336.1}.
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DR EMBL; LSTO01000001; OWW22336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254TI69; -.
DR OrthoDB; 5290247at2; -.
DR Proteomes; UP000197535; Unassembled WGS sequence.
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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd03218; ABC_YhbG; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR032823; BCA_ABC_TP_C.
DR InterPro; IPR030921; LPS_export_LptB.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR04406; LPS_export_lptB; 1.
DR PANTHER; PTHR45772; CONSERVED COMPONENT OF ABC TRANSPORTER FOR NATURAL AMINO ACIDS-RELATED; 1.
DR PANTHER; PTHR45772:SF10; LIPOPOLYSACCHARIDE EXPORT SYSTEM ATP-BINDING PROTEIN LPTB; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF12399; BCA_ABC_TP_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:OWW22336.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000197535};
KW Translocase {ECO:0000256|ARBA:ARBA00022967}.
FT DOMAIN 5..242
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 246 AA; 27158 MW; 82B70044B330E516 CRC64;
MTSTLVVNGL QKSYGTRQVV RDVSLQVASG EVVGLLGPNG AGKTTSFYMI VGLVPSDAGE
IDLNGVGISR LPIHRRATLG LSYLPQEASV FRKLSVEDNI RAVLELQRID DKPLPKAEIE
KRLNTLLAEL QIERLRENQA LSLSGGERRR VEIARALATN PRFVLLDEPF AGVDPIAVIE
IQRIVRFLKE RGIGVLITDH NVRETLGICD RAYIINQGSV LASGRPDDII ANESVRRVYL
GEHFRM
//
