ID A0A0K0XVK5_9GAMM Unreviewed; 387 AA.
AC A0A0K0XVK5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN ORFNames=HNQ63_000972 {ECO:0000313|EMBL:MBB6086535.1}, WM2015_1331
GN {ECO:0000313|EMBL:AKS41703.1};
OS Wenzhouxiangella marina.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Wenzhouxiangellaceae; Wenzhouxiangella.
OX NCBI_TaxID=1579979 {ECO:0000313|EMBL:AKS41703.1, ECO:0000313|Proteomes:UP000066624};
RN [1] {ECO:0000313|EMBL:AKS41703.1, ECO:0000313|Proteomes:UP000066624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42284 {ECO:0000313|EMBL:AKS41703.1,
RC ECO:0000313|Proteomes:UP000066624};
RA Noorani M.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB6086535.1, ECO:0000313|Proteomes:UP000581413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 103414 {ECO:0000313|EMBL:MBB6086535.1,
RC ECO:0000313|Proteomes:UP000581413};
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 (AUG-2020) 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}.
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DR EMBL; CP012154; AKS41703.1; -; Genomic_DNA.
DR EMBL; JACHIC010000001; MBB6086535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0K0XVK5; -.
DR STRING; 1579979.WM2015_1331; -.
DR KEGG; wma:WM2015_1331; -.
DR PATRIC; fig|1579979.3.peg.1365; -.
DR OrthoDB; 507476at2; -.
DR Proteomes; UP000066624; Chromosome.
DR Proteomes; UP000581413; 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; 3.
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; 5.
DR SUPFAM; SSF48452; TPR-like; 1.
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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00994}; Reference proteome {ECO:0000313|Proteomes:UP000066624};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW Stress response {ECO:0000313|EMBL:AKS41703.1};
KW TPR repeat {ECO:0000256|HAMAP-Rule:MF_00994, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00994};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994}.
FT TOPO_DOM 23..387
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT REPEAT 108..141
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 353..377
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
FT BINDING 355
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 358
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 369
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"
SQ SEQUENCE 387 AA; 44418 MW; 327F3995B67617F1 CRC64;
MAELALLFLL LPVAAATGWW VARRGERARR SRSSALSSSY FRGLNYLLNE QPDKAIEVFL
ELADINPDTV ETHLALGNLF RRRGEMDKAI RFHKHIMTRP NLSDEQRALA LYELGEDYMQ
AGLLDRAERL FRELAEHDSN NVVPTRQLLS IYQQEKDWEQ AIEMARTLRE DGPERGELIA
QFQCEIAAQA LNDNDTERAR QALRQARRYD PRNPRARLLE GDLAWSMEDW SRAADHYRAA
CDLDADCLIQ VLERIIECHR RVDDPDALDD WLQTVVERSP MTTPLIALAQ RRAANDPQGA
ADLVLDRMAR RPTVRGLKYL MSLLVSEGAR LDRIDPALVG DLLDRLLSDQ PLYRCQHCGF
SGTSYHWLCP SCRRWNTTRA IRGILGE
//
