LAPB_HAEIN
ID LAPB_HAEIN Reviewed; 396 AA.
AC P44130;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000255|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000255|HAMAP-Rule:MF_00994}; OrderedLocusNames=HI_1223;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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:0000255|HAMAP-Rule:MF_00994}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00994}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00994}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00994}.
CC -!- SIMILARITY: Belongs to the LapB family. {ECO:0000255|HAMAP-
CC Rule:MF_00994}.
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DR EMBL; L42023; AAC22876.1; -; Genomic_DNA.
DR PIR; D64022; D64022.
DR RefSeq; NP_439379.1; NC_000907.1.
DR RefSeq; WP_005694286.1; NC_000907.1.
DR AlphaFoldDB; P44130; -.
DR SMR; P44130; -.
DR STRING; 71421.HI_1223; -.
DR PRIDE; P44130; -.
DR EnsemblBacteria; AAC22876; AAC22876; HI_1223.
DR KEGG; hin:HI_1223; -.
DR PATRIC; fig|71421.8.peg.1275; -.
DR eggNOG; COG2956; Bacteria.
DR HOGENOM; CLU_059365_1_0_6; -.
DR OMA; FWQCPGC; -.
DR PhylomeDB; P44130; -.
DR BioCyc; HINF71421:G1GJ1-1254-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031235; C:intrinsic component of the cytoplasmic side of the 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; -; 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 Pfam; PF18073; Rubredoxin_2; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR PROSITE; PS50005; TPR; 3.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding;
KW Reference proteome; Repeat; TPR repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..396
FT /note="Lipopolysaccharide assembly protein B"
FT /id="PRO_0000013831"
FT TRANSMEM 1..20
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT TOPO_DOM 21..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 35..68
FT /note="TPR 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 77..109
FT /note="TPR 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 149..182
FT /note="TPR 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 221..254
FT /note="TPR 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 364
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 367
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 378
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 381
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
SQ SEQUENCE 396 AA; 45627 MW; E743D4A56B34334F CRC64;
MIELLFLLLP IAAAYGWYMG RRSAKKDQDD ISNKLSRDYV TGVNFLLSNQ TDKAVDLFLD
MLQKQEIENE IESHSQFEAE LTLGNLFRSR GEVDRALRIH QALDLSPNYT FEQKLLAKQQ
LARDFMVVGF FDRAENLYIL LVDEPEFAEN ALQQLLVIYQ KTKEWKKAVN IAEKLAKIKP
QENNIELAQC YCEYSQSLEP ESAVEKRSVL QKALSVSPTC VRASLLLANL AMLDGQYQQA
VKILENVLEQ NPDYTGEILL PLKHCYEELN QLDNFELFLI RAGQIINNDE VELALAKLIE
EKDGKSAAQA KLYQQLTKKP STLIFHRFMQ YQIDDAEDGR GKESLILLHK MVGERIKQTS
PYRCTNCGYQ IHKLLWNCPS CRQWESIKPV SNQEHN
