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
//