LAPB_ECOL6
ID LAPB_ECOL6 Reviewed; 389 AA.
AC P0AB59; P45576; P76836;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000255|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000255|HAMAP-Rule:MF_00994}; Synonyms=yciM;
GN OrderedLocusNames=c1749;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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; AE014075; AAN80215.1; -; Genomic_DNA.
DR RefSeq; WP_000891353.1; NC_004431.1.
DR AlphaFoldDB; P0AB59; -.
DR SMR; P0AB59; -.
DR STRING; 199310.c1749; -.
DR EnsemblBacteria; AAN80215; AAN80215; c1749.
DR GeneID; 58460487; -.
DR KEGG; ecc:c1749; -.
DR eggNOG; COG2956; Bacteria.
DR HOGENOM; CLU_059365_1_0_6; -.
DR OMA; FWQCPGC; -.
DR BioCyc; ECOL199310:C1749-MON; -.
DR Proteomes; UP000001410; 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; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding; Repeat;
KW TPR repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..389
FT /note="Lipopolysaccharide assembly protein B"
FT /id="PRO_0000042576"
FT TRANSMEM 1..20
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT TOPO_DOM 21..389
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 69..102
FT /note="TPR 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 107..140
FT /note="TPR 3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 142..174
FT /note="TPR 4"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 180..213
FT /note="TPR 5"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 214..247
FT /note="TPR 6"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT REPEAT 249..282
FT /note="TPR 7"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 360
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 371
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
FT BINDING 374
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994"
SQ SEQUENCE 389 AA; 44531 MW; F4D1B9E2A526BCC3 CRC64;
MLELLFLLLP VAAAYGWYMG RRSAQQNKQD EANRLSRDYV AGVNFLLSNQ QDKAVDLFLD
MLKEDTGTVE AHLTLGNLFR SRGEVDRAIR IHQTLMESAS LTYEQRLLAI QQLGRDYMAA
GLYDRAEDMF NQLTDETDFR IGALQQLLQI YQATSEWQKA IDVAERLVKL GKDKQRVEIA
HFYCELALQH MASDDLDRAM TLLKKGAAAD KNSARVSIMM GRVFMAKGEY AKAVESLQRV
ISQDRELVSE TLEMLQTCYQ QLGKTAEWAE FLQRAVEENT GADAELMLAD IIEARDGSEA
AQVYITRQLQ RHPTMRVFHK LMDYHLNEAE EGRAKESLMV LRDMVGEKVR SKPRYRCQKC
GFTAYTLYWH CPSCRAWSTI KPIRGLDGL
