LAPB_ECOLI
ID LAPB_ECOLI Reviewed; 389 AA.
AC P0AB58; P45576; P76836;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000303|PubMed:24722986};
DE AltName: Full=Lipopolysaccharide regulatory protein {ECO:0000255|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000303|PubMed:24722986};
GN Synonyms=yciM; OrderedLocusNames=b1280, JW1272;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 308-389.
RX PubMed=3052852; DOI=10.1016/0092-8674(88)90033-5;
RA Hidaka M., Akiyama M., Horiuchi T.;
RT "A consensus sequence of three DNA replication terminus sites on the E.
RT coli chromosome is highly homologous to the terR sites of the R6K
RT plasmid.";
RL Cell 55:467-475(1988).
RN [5]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [6]
RP SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE, DOMAIN, IRON-BINDING,
RP AND MUTAGENESIS OF CYS-184; CYS-258; CYS-357; CYS-360; CYS-371 AND CYS-374.
RC STRAIN=K12 / MC1000 / ATCC 39531;
RX PubMed=24187084; DOI=10.1128/jb.00921-13;
RA Nicolaes V., El Hajjaji H., Davis R.M., Van der Henst C., Depuydt M.,
RA Leverrier P., Aertsen A., Haufroid V., Ollagnier de Choudens S.,
RA De Bolle X., Ruiz N., Collet J.F.;
RT "Insights into the function of YciM, a heat shock membrane protein required
RT to maintain envelope integrity in Escherichia coli.";
RL J. Bacteriol. 196:300-309(2014).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF CYS-371; PRO-372 AND SER-378.
RX PubMed=24722986; DOI=10.1074/jbc.m113.539494;
RA Klein G., Kobylak N., Lindner B., Stupak A., Raina S.;
RT "Assembly of lipopolysaccharide in Escherichia coli requires the essential
RT LapB heat shock protein.";
RL J. Biol. Chem. 289:14829-14853(2014).
RN [8]
RP FUNCTION, AND INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=24266962; DOI=10.1111/mmi.12452;
RA Mahalakshmi S., Sunayana M.R., SaiSree L., Reddy M.;
RT "yciM is an essential gene required for regulation of lipopolysaccharide
RT synthesis in Escherichia coli.";
RL Mol. Microbiol. 91:145-157(2014).
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 ECO:0000269|PubMed:24266962, ECO:0000269|PubMed:24722986}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00994, ECO:0000269|PubMed:24187084,
CC ECO:0000269|PubMed:24722986}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00994, ECO:0000269|PubMed:24187084};
CC Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_00994,
CC ECO:0000269|PubMed:24187084}.
CC -!- INDUCTION: Induced by heat shock, via RpoH.
CC {ECO:0000269|PubMed:24266962, ECO:0000269|PubMed:24722986}.
CC -!- DOMAIN: The membrane anchor N-terminal domain is required for activity.
CC The iron-binding domain is required for protein stability and function.
CC {ECO:0000269|PubMed:24187084}.
CC -!- DISRUPTION PHENOTYPE: Deletion leads to changes in cell morphology and
CC to the formation of bulges that contain cytoplasmic material and cause
CC cell lysis. Mutants exhibit increased sensitivity to rifampicin and
CC novobiocin, and to a mixture of SDS and EDTA. Growth is severely
CC affected by osmolarity and temperature (PubMed:24187084). Mutant
CC accumulates precursor forms of LPS and exhibits elevated levels of LpxC
CC (PubMed:24722986). {ECO:0000269|PubMed:24187084,
CC ECO:0000269|PubMed:24722986}.
CC -!- SIMILARITY: Belongs to the LapB family. {ECO:0000255|HAMAP-
CC Rule:MF_00994, ECO:0000305}.
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DR EMBL; U00096; AAC74362.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14834.1; -; Genomic_DNA.
DR EMBL; M23250; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64876; C64876.
DR RefSeq; NP_415796.1; NC_000913.3.
DR RefSeq; WP_000891353.1; NZ_STEB01000005.1.
DR AlphaFoldDB; P0AB58; -.
DR SMR; P0AB58; -.
DR BioGRID; 4259400; 56.
DR DIP; DIP-48161N; -.
DR IntAct; P0AB58; 1.
DR STRING; 511145.b1280; -.
DR jPOST; P0AB58; -.
DR PaxDb; P0AB58; -.
DR PRIDE; P0AB58; -.
DR EnsemblBacteria; AAC74362; AAC74362; b1280.
DR EnsemblBacteria; BAA14834; BAA14834; BAA14834.
DR GeneID; 58460487; -.
DR GeneID; 944858; -.
DR KEGG; ecj:JW1272; -.
DR KEGG; eco:b1280; -.
DR PATRIC; fig|1411691.4.peg.1001; -.
DR EchoBASE; EB2554; -.
DR eggNOG; COG2956; Bacteria.
DR HOGENOM; CLU_059365_1_0_6; -.
DR InParanoid; P0AB58; -.
DR OMA; FWQCPGC; -.
DR PhylomeDB; P0AB58; -.
DR BioCyc; EcoCyc:EG12691-MON; -.
DR PRO; PR:P0AB58; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
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:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0051301; P:cell division; IBA:GO_Central.
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 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Iron; Membrane; Metal-binding;
KW Reference proteome; Repeat; Stress response; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..389
FT /note="Lipopolysaccharide assembly protein B"
FT /id="PRO_0000013830"
FT TRANSMEM 1..20
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994,
FT ECO:0000269|PubMed:24187084"
FT TOPO_DOM 21..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994,
FT ECO:0000269|PubMed:24187084"
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 ECO:0000269|PubMed:24187084"
FT BINDING 360
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994,
FT ECO:0000269|PubMed:24187084"
FT BINDING 371
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994,
FT ECO:0000269|PubMed:24187084"
FT BINDING 374
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00994,
FT ECO:0000269|PubMed:24187084"
FT MUTAGEN 184
FT /note="C->S: Does not affect metal binding; when associated
FT with S-258."
FT /evidence="ECO:0000269|PubMed:24187084"
FT MUTAGEN 258
FT /note="C->S: Does not affect metal binding; when associated
FT with S-184."
FT /evidence="ECO:0000269|PubMed:24187084"
FT MUTAGEN 357
FT /note="C->S: Lack of activity; when associated with S-360;
FT S-371 and S-374."
FT /evidence="ECO:0000269|PubMed:24187084"
FT MUTAGEN 360
FT /note="C->S: Lack of activity; when associated with S-357;
FT S-371 and S-374."
FT /evidence="ECO:0000269|PubMed:24187084"
FT MUTAGEN 371
FT /note="C->R: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24722986"
FT MUTAGEN 371
FT /note="C->S: Lack of activity; when associated with S-357;
FT S-360 and S-374."
FT /evidence="ECO:0000269|PubMed:24187084"
FT MUTAGEN 372
FT /note="P->L: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24722986"
FT MUTAGEN 374
FT /note="C->S: Lack of activity; when associated with S-357;
FT S-360 and S-371."
FT /evidence="ECO:0000269|PubMed:24187084"
FT MUTAGEN 378
FT /note="S->P: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24722986"
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
