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Database: UniProt
Entry: A0A0S2KFE4_9GAMM
LinkDB: A0A0S2KFE4_9GAMM
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ID   A0A0S2KFE4_9GAMM        Unreviewed;       241 AA.
AC   A0A0S2KFE4;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Lipopolysaccharide export system ATP-binding protein LptB {ECO:0000256|ARBA:ARBA00017803};
GN   ORFNames=PS2015_2335 {ECO:0000313|EMBL:ALO46969.1};
OS   Pseudohongiella spirulinae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudohongiella.
OX   NCBI_TaxID=1249552 {ECO:0000313|EMBL:ALO46969.1, ECO:0000313|Proteomes:UP000065641};
RN   [1] {ECO:0000313|EMBL:ALO46969.1, ECO:0000313|Proteomes:UP000065641}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 32221 {ECO:0000313|EMBL:ALO46969.1,
RC   ECO:0000313|Proteomes:UP000065641};
RA   Zhang Y., Guo Z.;
RL   Submitted (NOV-2015) 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}.
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DR   EMBL; CP013189; ALO46969.1; -; Genomic_DNA.
DR   RefSeq; WP_058022408.1; NZ_CP013189.1.
DR   AlphaFoldDB; A0A0S2KFE4; -.
DR   STRING; 1249552.PS2015_2335; -.
DR   KEGG; pspi:PS2015_2335; -.
DR   PATRIC; fig|1249552.3.peg.2348; -.
DR   OrthoDB; 9781337at2; -.
DR   Proteomes; UP000065641; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
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:ALO46969.1};
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:UP000065641}.
FT   DOMAIN          4..237
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   241 AA;  26716 MW;  D41F4EB43FBD23EF CRC64;
     MDILNAFNLA KSYKGRQVVR DVSMSVRSGE IVGLLGPNGA GKTTCFYMIV GLVNADRGRI
     LINDENLTGL PIFARARLGL GYLPQDSSIF RNLSVEDNIM AILETRNDLD KAGRQEKLDS
     LIQEFHINHI RKNKGMSLSG GERRRTEIAR ALANDPRFIL LDEPFAGVDP ISVSDIKSII
     EHLKQRGIGV LLTDHNVRET LDICDKAYIV SEGGIIAEGS SEQILANEKV REVYLGKNFH
     I
//
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