ID A0A3S0JZY5_9GAMM Unreviewed; 394 AA.
AC A0A3S0JZY5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 17.
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:RTR06514.1};
GN ORFNames=EKG36_03320 {ECO:0000313|EMBL:RTR06514.1};
OS Halomonas nitroreducens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=447425 {ECO:0000313|EMBL:RTR06514.1, ECO:0000313|Proteomes:UP000267400};
RN [1] {ECO:0000313|EMBL:RTR06514.1, ECO:0000313|Proteomes:UP000267400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=11S {ECO:0000313|EMBL:RTR06514.1,
RC ECO:0000313|Proteomes:UP000267400};
RA Yu L.;
RL Submitted (DEC-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:RTR06514.1}.
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DR EMBL; RXNS01000002; RTR06514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S0JZY5; -.
DR OrthoDB; 507476at2; -.
DR Proteomes; UP000267400; 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; IPR016024; ARM-type_fold.
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; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF48452; TPR-like; 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}; 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 22..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT DOMAIN 360..386
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
FT BINDING 362
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 376
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 379
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ SEQUENCE 394 AA; 44809 MW; 60C0A394D3C061A2 CRC64;
MRDALLLALL LAAVAIGWWL GRRERRSPGT PATSPGLARD YFVGLNYLLN DQQDRAIETF
VGALEVNSDT IETHIALGNL FRSRGEADRA VKIHQNLLAR PTLTGDQGER VQLELSRDFL
HLGLLDRAER LLQGLVKDGQ DDELRLSARR LLVDLLEREG EWQAALDVAL PNLVRQHDDI
RRAAAHWLCE LADQERRSAS PVLARRHLKQ ALTTDARCVR ANLLLAEMAL DTGQYRQSIR
LLKRIPDQDK TFIPSMLEPL SRAYRLLDDE AGLIQYLEEL LETTPYTSVI ILLAETLRRH
DGDARAAHEL VARQLNREPS LGAVDYLIRL YLRDAPGGDD ERIELLQRHT QTLLKSLPRH
RCRRCGFSGE HLHWRCPRCR SWGTTKPITG IEGE
//
