ID A0A257EHB5_9BURK Unreviewed; 389 AA.
AC A0A257EHB5;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN ORFNames=CFE38_03315 {ECO:0000313|EMBL:OYU13308.1};
OS Comamonadaceae bacterium PBBC1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=2015580 {ECO:0000313|EMBL:OYU13308.1, ECO:0000313|Proteomes:UP000216161};
RN [1] {ECO:0000313|EMBL:OYU13308.1, ECO:0000313|Proteomes:UP000216161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBBC1 {ECO:0000313|EMBL:OYU13308.1};
RA Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT formosa and its bacterial cohort.";
RL Submitted (JUN-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}.
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:OYU13308.1}.
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DR EMBL; NKIP01000002; OYU13308.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A257EHB5; -.
DR Proteomes; UP000216161; 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; 1.
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 Pfam; PF18073; Rubredoxin_2; 1.
DR Pfam; PF13432; TPR_16; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; TPR-like; 2.
DR PROSITE; PS50005; TPR; 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}; Repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW TPR repeat {ECO:0000256|HAMAP-Rule:MF_00994, ECO:0000256|PROSITE-
KW ProRule:PRU00339};
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..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT REPEAT 37..70
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 356..380
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
FT BINDING 358
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 361
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 372
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 375
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ SEQUENCE 389 AA; 43341 MW; 53E1FC0F2F1F3AB5 CRC64;
MEFDLTWILL GLPAAFALGW IASRLDLRQM RIANRQAPRA YFKGLNYLLN EQQDQAIDAF
IEAVQNDPDT SELHFALGNL FRRRGEYDRA VRVHEHLLQR ADISTADRQR AQHGLALDYL
KAGLLDRAEE ALRKLEGTSY EGQARLARMA IYERSREWPE AAAVARLLEK SGESNFGIRL
AHYQCEQARE AVQKGDSAKA LALLAQSLKE QSEAARPRIL QGQLLLSQGQ AVPAYASLAV
LFERNDMAAP LAAASLAQAA QACGKADEAL ALLQAHYQRQ PCIDVLDAIM TLSANPSPAD
QLTQAQAMQR YLDHLQKTPS LMAASRWLNG VQPSDHALPA PVQKALEHAT KPLARYRCAA
CGFEAKEHFW HCPGCQAWDS YPPRRIEEL
//
