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Database: UniProt
Entry: A0A3N6Q3L9_9BURK
LinkDB: A0A3N6Q3L9_9BURK
Original site: A0A3N6Q3L9_9BURK 
ID   A0A3N6Q3L9_9BURK        Unreviewed;       391 AA.
AC   A0A3N6Q3L9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994,
GN   ECO:0000313|EMBL:RQH09720.1};
GN   ORFNames=D1Y85_00770 {ECO:0000313|EMBL:RQH09720.1};
OS   Paraburkholderia dinghuensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2305225 {ECO:0000313|EMBL:RQH09720.1, ECO:0000313|Proteomes:UP000272778};
RN   [1] {ECO:0000313|EMBL:RQH09720.1, ECO:0000313|Proteomes:UP000272778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHOA04 {ECO:0000313|EMBL:RQH09720.1,
RC   ECO:0000313|Proteomes:UP000272778};
RA   Gao Z.-H., Qiu L.-H., Fu J.-C.;
RT   "Paraburkholderia sp. DHOA04, isolated from soil.";
RL   Submitted (NOV-2018) 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}.
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:RQH09720.1}.
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DR   EMBL; RQIS01000001; RQH09720.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N6Q3L9; -.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000272778; Unassembled WGS sequence.
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:SF17; LIPOPOLYSACCHARIDE ASSEMBLY PROTEIN B; 1.
DR   PANTHER; PTHR45586; TPR REPEAT-CONTAINING PROTEIN PA4667; 1.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   Pfam; PF13432; TPR_16; 2.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; TPR-like; 2.
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:UP000272778};
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..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        23..391
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   DOMAIN          354..378
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         356
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         359
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         370
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         373
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ   SEQUENCE   391 AA;  44071 MW;  237AF00F58F4471B CRC64;
     MDLDFWWLLV IPVAFALGWM ASRYDLKALL SESANLPRSY FRGLNFLLNE QPDKAIDAFI
     EVAKLDPETV ELHFALGNLF RRRGETDRAI RVHQNLLSRP DLPVNERDHA LYELGQDYLK
     AGLLDRAEET FVSLQSGDYA QGAQRALLTI YEIEKDWNRS IDTARQLEKM GAGSLDLEIA
     QFHCELAQEA LQQKKPDEAR RQLAFALKAN PQNVRATILG GDVDAASGAG ESALAQWRRV
     EEQNPAYLPL VAEKVMKAYE TLGRADEGAQ LLTQWVDAYP SNDLLDVAYK YVAALRGADA
     AHALARAQMQ KSPNLAGMSR LLEAQQAAAE EPRRSELELM RSLLQQRTKN LPRYTCQNCG
     FRARLFYWQC PGCSGWETYA PRRVEPVPAS N
//
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