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Database: UniProt
Entry: D3VDI0_XENNA
LinkDB: D3VDI0_XENNA
Original site: D3VDI0_XENNA 
ID   D3VDI0_XENNA            Unreviewed;       241 AA.
AC   D3VDI0;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB {ECO:0000256|ARBA:ARBA00017803};
GN   Name=yhbG {ECO:0000313|EMBL:CBJ92220.1};
GN   OrderedLocusNames=XNC1_4195 {ECO:0000313|EMBL:CBJ92220.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / CCUG 14189 / LMG
OS   1036 / NCIMB 9965 / AN6).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ92220.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|EMBL:CBJ92220.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / CCUG 14189 / LMG 1036 / NCIMB 9965 /
RC   AN6 {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C., de Leon L.,
RA   Drace K., Du Z., Givaudan A., Herbert Tran E.E., Jewell K.A., Knack J.J.,
RA   Krasomil-Osterfeld K.C., Kukor R., Lanois A., Latreille P.,
RA   Leimgruber N.K., Lipke C.M., Liu R., Lu X., Martens E.C., Marri P.R.,
RA   Medigue C., Menard M.L., Miller N.M., Morales-Soto N., Norton S.,
RA   Ogier J.C., Orchard S.S., Park D., Park Y., Qurollo B.A., Sugar D.R.,
RA   Richards G.R., Rouy Z., Slominski B., Slominski K., Snyder H., Tjaden B.C.,
RA   van der Hoeven R., Welch R.D., Wheeler C., Xiang B., Barbazuk B.,
RA   Gaudriault S., Goodner B., Slater S.C., Forst S., Goldman B.S.,
RA   Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and photorhabdus:
RT   convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:E27909-E27909(2011).
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}.
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DR   EMBL; FN667742; CBJ92220.1; -; Genomic_DNA.
DR   RefSeq; WP_013185524.1; NC_014228.1.
DR   AlphaFoldDB; D3VDI0; -.
DR   STRING; 406817.XNC1_4195; -.
DR   KEGG; xne:XNC1_4195; -.
DR   eggNOG; COG1137; Bacteria.
DR   HOGENOM; CLU_000604_1_2_6; -.
DR   Proteomes; UP000008075; Chromosome.
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};
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:UP000008075}.
FT   DOMAIN          4..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   241 AA;  26872 MW;  DDB5140C2656CC3C CRC64;
     MAILNAENLA KAYKGRKVVE NVSLEVKSGE IVGLLGPNGA GKTTTFYMVV GIVPRDAGSI
     TIDQEDISLL PLHERARRGI GYLPQEASIF RRLSVFNNLM AVLEIRKDLN QEQQKVRAEE
     LMEEFHISHL RDSLGQSLSG GERRRVEIAR ALAANPKFIL LDEPFAGVDP ISVLDIKKII
     QHLRDYGLGV LITDHNVRET LDVCERAYIV SQGHLIAHGS PDDILNNEQV KRVYLGEGFR
     L
//
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