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Database: UniProt
Entry: A0A318H2J9_9BURK
LinkDB: A0A318H2J9_9BURK
Original site: A0A318H2J9_9BURK 
ID   A0A318H2J9_9BURK        Unreviewed;       382 AA.
AC   A0A318H2J9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   18-JUN-2025, entry version 19.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN   ORFNames=C7444_12716 {ECO:0000313|EMBL:PXW92261.1};
OS   Sphaerotilus hippei.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Sphaerotilaceae; Sphaerotilus.
OX   NCBI_TaxID=744406 {ECO:0000313|EMBL:PXW92261.1, ECO:0000313|Proteomes:UP000247811};
RN   [1] {ECO:0000313|EMBL:PXW92261.1, ECO:0000313|Proteomes:UP000247811}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 566 {ECO:0000313|EMBL:PXW92261.1,
RC   ECO:0000313|Proteomes:UP000247811};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAY-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:PXW92261.1}.
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DR   EMBL; QJJS01000027; PXW92261.1; -; Genomic_DNA.
DR   RefSeq; WP_110402441.1; NZ_QJJS01000027.1.
DR   AlphaFoldDB; A0A318H2J9; -.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000247811; 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_rpt.
DR   NCBIfam; NF008755; PRK11788.1-3; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13176; TPR_7; 1.
DR   Pfam; PF18073; Zn_ribbon_LapB; 1.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00994}; Reference proteome {ECO:0000313|Proteomes:UP000247811};
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};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994}.
FT   TOPO_DOM        24..382
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   DOMAIN          349..373
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         351
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         354
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         365
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"
SQ   SEQUENCE   382 AA;  42430 MW;  CDBCAA637621CDC8 CRC64;
     MDFELQWLLM GLPVAFALGW LASRLDLRQW KHEVESSPRA YFKGLNLLLN EQQDKAIDAF
     IEAVQHDPGS SDLHFALGNL FRRRGDYERA VRVHQHVLGR ADLPVAERDR AQHALAQDYL
     KAGLFDRAEA AYQQLEGTAF ATDARLALLT LYERSRDWRQ ALEVARGLEA VAAGSFAGRI
     SHYWCEIALE AEAQGQLDDA QSALQRAREA APQAARPLVL LGQRQLRREQ PAEAMATWAL
     LATIHPDAFS VVAADYAAAA TACGAQAVAM ELLQGLLKQS PSSDVLAAWL KLAPEHAQRR
     EALLQALQHQ ASLSPALALL QDTPQVADEA AQQAIVRSMT AALKPLRRYR CAACGFEAHH
     YFWQCPGCQG WDTYPPRRLE DQ
//
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