ID I3DCI6_9PAST Unreviewed; 402 AA.
AC I3DCI6;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN ORFNames=HMPREF1052_0885 {ECO:0000313|EMBL:EIJ69429.1};
OS Pasteurella bettyae CCUG 2042.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=1095749 {ECO:0000313|EMBL:EIJ69429.1, ECO:0000313|Proteomes:UP000006457};
RN [1] {ECO:0000313|EMBL:EIJ69429.1, ECO:0000313|Proteomes:UP000006457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 2042 {ECO:0000313|EMBL:EIJ69429.1,
RC ECO:0000313|Proteomes:UP000006457};
RA Harkins D.M., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Nelson K.E.;
RL Submitted (MAR-2012) 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:EIJ69429.1}.
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DR EMBL; AJSX01000030; EIJ69429.1; -; Genomic_DNA.
DR RefSeq; WP_005760578.1; NZ_AJSX01000030.1.
DR AlphaFoldDB; I3DCI6; -.
DR PATRIC; fig|1095749.3.peg.1084; -.
DR eggNOG; COG2956; Bacteria.
DR OrthoDB; 507476at2; -.
DR Proteomes; UP000006457; 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; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 2.
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:UP000006457};
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..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT REPEAT 149..182
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 367..394
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
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"
FT BINDING 383
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 386
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ SEQUENCE 402 AA; 46694 MW; 0AC7CDEB2F009F1C CRC64;
MLELLFLLLP IAAAYGWYMG HRSAKKDQED VSNKLSRDYV TGVNFLLSNQ TDKAVDLFLD
MLQKQEAENE IESNSQFEAE LTLGNLFRSR GEVDRALRIH QNLDRSQHYS FEQKLLAKQQ
LAKDFMVMGF FDRAESIYIM LVDEPDFAES ALQQLAVIYQ KTKDWKKAIN VAEKLAKIAP
REDNIELAQY YCEYAKALHK ENKDTKEQQP KALLKQALHV LPRCVRASIL LGDILIKEQH
YQEAIVVLEN VLAQDATYLG EVVTRLKDCY HHLDQLDNFE IFLIRANQEC QYNSTVALAL
ADLIEEKHGR AAAQNKIYQQ LTHNPSLFLF YRFVEYQVEE AEDGRGKESL ILLRNLVGER
IKRNFDYRCS KCGYQSHKLI WCCPSCRQWE TIKPIRGIES QI
//
