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Database: UniProt
Entry: A0A2U2I4R2_9BURK
LinkDB: A0A2U2I4R2_9BURK
Original site: A0A2U2I4R2_9BURK 
ID   A0A2U2I4R2_9BURK        Unreviewed;       391 AA.
AC   A0A2U2I4R2;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN   ORFNames=C7C56_006455 {ECO:0000313|EMBL:PWF54575.1};
OS   Massilia glaciei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1524097 {ECO:0000313|EMBL:PWF54575.1, ECO:0000313|Proteomes:UP000241421};
RN   [1] {ECO:0000313|EMBL:PWF54575.1, ECO:0000313|Proteomes:UP000241421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B448-2 {ECO:0000313|EMBL:PWF54575.1,
RC   ECO:0000313|Proteomes:UP000241421};
RA   Wang H.;
RT   "Massilia violaceinigra sp. nov., a novel purple-pigmented bacterium
RT   isolated from Tianshan glacier, Xinjiang, China.";
RL   Submitted (APR-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:PWF54575.1}.
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DR   EMBL; PXWF02000083; PWF54575.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U2I4R2; -.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000241421; 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   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; 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:UP000241421};
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..24
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;  44508 MW;  F54833C73855C8BC CRC64;
     MDFELWWLLG IPVFFGLGWV AARVDIKQLV SESRTLPSGY FKGLNFLLNE QPDKAIDAFI
     EIVKLDSESA DMHFALGNLF RRRGEIERAI RVHQNLLARP DLPQEQQMQA QYELGMDYLK
     AGLLDRAEET FNQLVETPYA VQARRSLLEI FQREKEWTRA IEAAVGLQES GAGERQKEIA
     QFYCELAQDA LVHLQVAEAM ALLDKALHAD RKNVRATMLT GDAQLAQGDI EGALLTWRRV
     EQQSVPHVAL VAGRLMDGYR KVGRPQEGVN LLRAYLAEAS SIDLIEVVFK AVLELDGVEA
     AKQLVVEELR RTPTLLGLDK LLEARMMDAP ANIFEELSMV KNLVHGYTQK LARYQCSHCG
     FKARQFYWQC PGCSRWETYP PRRTEELNVM N
//
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