ID A0A1E5D8I5_9VIBR Unreviewed; 389 AA.
AC A0A1E5D8I5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN ORFNames=A130_10750 {ECO:0000313|EMBL:OEE80027.1};
OS Vibrio genomosp. F6 str. FF-238.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1191298 {ECO:0000313|EMBL:OEE80027.1, ECO:0000313|Proteomes:UP000094165};
RN [1] {ECO:0000313|EMBL:OEE80027.1, ECO:0000313|Proteomes:UP000094165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF-238 {ECO:0000313|EMBL:OEE80027.1,
RC ECO:0000313|Proteomes:UP000094165};
RX PubMed=22955834; DOI=10.1126/science.1219385;
RA Cordero O.X., Wildschutte H., Kirkup B., Proehl S., Ngo L., Hussain F.,
RA Le Roux F., Mincer T., Polz M.F.;
RT "Ecological populations of bacteria act as socially cohesive units of
RT antibiotic production and resistance.";
RL Science 337:1228-1231(2012).
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:OEE80027.1}.
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DR EMBL; AJYW02000014; OEE80027.1; -; Genomic_DNA.
DR RefSeq; WP_017053901.1; NZ_AJYW02000014.1.
DR AlphaFoldDB; A0A1E5D8I5; -.
DR Proteomes; UP000094165; 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_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; PF14559; TPR_19; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF81901; HCP-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:UP000094165};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00994};
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 21..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT REPEAT 214..247
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 355..382
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
FT BINDING 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 360
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"
FT BINDING 374
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ SEQUENCE 389 AA; 44329 MW; E4BD14067B3FFE8B CRC64;
MLELLFLLLP IAAAYGWYMG NRSAQQDKQT QSHQISRQYV TGLNLLLSDQ SDKAVDHFIE
LLQVDDDTID THLALGNLFR SRGEVDRAIR IHQNLISRTG LTLEQKNLAL QQLAKDYMVS
GFLDRAEKIF EQLVEEPEHK ESALQQLVTI YQQTKEWSKA IHYATALVKM GRKRVKSQIA
HFLCELAMQE QGEGQTNKAI QHFKKALVED PKCARASISL GKLYLESEDY QQTIKYMEMV
LNQDIDFISE VLPTLADCYH HLGQEEGLVE FLRACIDKKA GVSAELMLAQ LVANHESIGT
AQELLTRQLV KNPTMKGFYR LIDYHIAEAE EGRAKDSLTT LQSMVGEQLK IKPHYRCRKC
GFSTHSMYWH CPSCKGWGTI KPIRGLDGE
//
