ID A0A1T0CHE3_9GAMM Unreviewed; 259 AA.
AC A0A1T0CHE3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB {ECO:0000256|ARBA:ARBA00017803};
GN ORFNames=B0682_03920 {ECO:0000313|EMBL:OOS21777.1};
OS Moraxella lincolnii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=90241 {ECO:0000313|EMBL:OOS21777.1, ECO:0000313|Proteomes:UP000191094};
RN [1] {ECO:0000313|EMBL:OOS21777.1, ECO:0000313|Proteomes:UP000191094}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 9405 {ECO:0000313|EMBL:OOS21777.1,
RC ECO:0000313|Proteomes:UP000191094};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Jaen-Luchoro D.,
RA Gonzales-Siles L., Karlsson R., Yazdan S., Boulund F., Johnning A.,
RA Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Moraxella lincolnii CCUG 9405T type strain.";
RL Submitted (FEB-2017) 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:OOS21777.1}.
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DR EMBL; MUYT01000004; OOS21777.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0CHE3; -.
DR STRING; 90241.B0682_03920; -.
DR OrthoDB; 9781337at2; -.
DR Proteomes; UP000191094; 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; 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; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:OOS21777.1};
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:UP000191094}.
FT DOMAIN 16..255
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 259 AA; 28596 MW; CADB7A67BA5FE2E2 CRC64;
MTSDAKFISN QSISKLSIRH LAKQYGKRWV VKDVSFELSQ GQVVGLLGPN GAGKTTSFYM
VVGLVPMDKG QVLLMDSEHG AGTSLSHLSM HERARHGIGY LPQEASIFRK LSIQDNILSI
LQTRKDLNKA EQKQTLEKLM AEFHLEHVRH SMGMSVSGGE RRRCEIARAL AANPKFILLD
EPFAGVDPIS VGDIKEVVTQ LKQRGIGVLI TDHNVRETLA ICEKAYIVSE GTIIAEGSAD
DILQNDLVRQ VYLGEDFVV
//
