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Database: UniProt
Entry: A0A1P8JTQ1_9BURK
LinkDB: A0A1P8JTQ1_9BURK
Original site: A0A1P8JTQ1_9BURK 
ID   A0A1P8JTQ1_9BURK        Unreviewed;       385 AA.
AC   A0A1P8JTQ1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN   ORFNames=RD110_07790 {ECO:0000313|EMBL:APW37108.1};
OS   Rhodoferax koreense.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=1842727 {ECO:0000313|EMBL:APW37108.1, ECO:0000313|Proteomes:UP000186609};
RN   [1] {ECO:0000313|EMBL:APW37108.1, ECO:0000313|Proteomes:UP000186609}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCY110 {ECO:0000313|EMBL:APW37108.1,
RC   ECO:0000313|Proteomes:UP000186609};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Modulates cellular lipopolysaccharide (LPS) levels by
CC       regulating LpxC, which is involved in lipid A biosynthesis. May act by
CC       modulating the proteolytic activity of FtsH towards LpxC. May also
CC       coordinate assembly of proteins involved in LPS synthesis at the plasma
CC       membrane. {ECO:0000256|HAMAP-Rule:MF_00994}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_00994}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_00994}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00994}.
CC   -!- SIMILARITY: Belongs to the LapB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00994}.
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DR   EMBL; CP019236; APW37108.1; -; Genomic_DNA.
DR   RefSeq; WP_076198260.1; NZ_CP019236.1.
DR   AlphaFoldDB; A0A1P8JTQ1; -.
DR   STRING; 1842727.RD110_07790; -.
DR   KEGG; rhy:RD110_07790; -.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000186609; Chromosome.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008653; P:lipopolysaccharide metabolic process; IEA:InterPro.
DR   GO; GO:0046890; P:regulation of lipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   HAMAP; MF_00994; LPS_assembly_LapB; 1.
DR   InterPro; IPR030865; LapB.
DR   InterPro; IPR041166; Rubredoxin_2.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45586:SF1; LIPOPOLYSACCHARIDE ASSEMBLY PROTEIN B; 1.
DR   PANTHER; PTHR45586; TPR REPEAT-CONTAINING PROTEIN PA4667; 1.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF13176; TPR_7; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; TPR-like; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_00994};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00994};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_00994};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00994, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00994}; Reference proteome {ECO:0000313|Proteomes:UP000186609};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW   TPR repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_00994, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        24..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   DOMAIN          352..376
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         354
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         357
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         368
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         371
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ   SEQUENCE   385 AA;  42855 MW;  2E9B99F293D7F8B3 CRC64;
     MDFDLGWILL GLPITFILGW LASRFDLRQL RVENRQAPKA YFKGLNFLLN EQQDQAIDAF
     IEAVQKDPDT SELHFALGNL FRRRGEYERA VRVHEHLLSR GDLSTVDRDR SQHALALDFL
     KAGLLDRAEA ALRKLEGTKY EAQSRLALLS IYERSRDWPK ASAIAKKLED AGQGSFNGRL
     AHYLCEQAAA LVASRQPEAA LLLLQQAIAT APQAPRPRID LAALQQQAGQ FGEAFATLQT
     LAETAPIAMP LIAPMIARVG TEAGRSAEAL ALLEASYAQS PSLDVLEAIV SLQSANPAEA
     AAARYRYVQH LDHEQSLVAA ARWIAGEKLE HEEFHPQVQR ALDHATKPLT RYRCAACGFE
     AKQHFWQCPG CQAWDSYPAR RVEEL
//
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