ID A0A2Z6ICE7_9BURK Unreviewed; 390 AA.
AC A0A2Z6ICE7;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
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:BBF24143.1};
GN ORFNames=SUTMEG_20340 {ECO:0000313|EMBL:BBF24143.1};
OS Sutterella megalosphaeroides.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sutterellaceae; Sutterella.
OX NCBI_TaxID=2494234 {ECO:0000313|EMBL:BBF24143.1, ECO:0000313|Proteomes:UP000271003};
RN [1] {ECO:0000313|EMBL:BBF24143.1, ECO:0000313|Proteomes:UP000271003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=6FBBBH3 {ECO:0000313|EMBL:BBF24143.1,
RC ECO:0000313|Proteomes:UP000271003};
RX PubMed=30394865; DOI=10.1099/ijsem.0.003096;
RA Sakamoto M., Ikeyama N., Kunihiro T., Iino T., Yuki M., Ohkuma M.;
RT "Mesosutterella multiformis gen. nov., sp. nov., a member of the family
RT Sutterellaceae and Sutterella megalosphaeroides sp. nov., isolated from
RT human faeces.";
RL Int. J. Syst. Evol. Microbiol. 68:3942-3950(2018).
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; AP018786; BBF24143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z6ICE7; -.
DR KEGG; sutt:SUTMEG_20340; -.
DR OrthoDB; 507476at2; -.
DR Proteomes; UP000271003; Chromosome.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042802; F:identical protein binding; IEA:InterPro.
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; IPR011717; TPR-4.
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; 1.
DR Pfam; PF07721; TPR_4; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 4.
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:UP000271003};
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..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT DOMAIN 352..378
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 390 AA; 43957 MW; 7769FD2B21EA4918 CRC64;
MEFDLWYLVA LPALFAAGWL CRGFDRRQRS EKTQLPEHFT RGVALLLDDE PDKAIDVLVE
ACRLDPDLIE LHHMLGKLFR RRGEFERAIR LHLHLVNRSD LSDADRTKAL SELAEDYFAA
GLFDRAEAEY RKLSEVPSEH LGALRRLLTI YTIEHEWESA IDTVRAVEAQ TGEDHRLETA
HFYCERIEVA LRSKRLEEAS KLVAEVLPYA DVTPRVDHLA GKVALAAGSV EEAAEHWRRL
ARNFPAHTPL VIGELADAMA ALGQKDEAIE LLRSALPEHP TADALEAVIA RVTEWRGLPE
AEAIAAKMLA AHPSLSAFNA LVRLRAKANP EDEQTKLLSG LLQRHAQRFA RYQCTHCGFL
ASNFAWHCLG CGSWDSFPPR RVEDSKGKSR
//
