LAPB_ECO57
ID LAPB_ECO57 Reviewed; 389 AA.
AC P0AB60; P45576; P76836;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 103.
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=Z2526, ECs1853;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG56533.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB35276.1; -; Genomic_DNA.
DR PIR; A85759; A85759.
DR PIR; E90860; E90860.
DR RefSeq; NP_309880.1; NC_002695.1.
DR RefSeq; WP_000891353.1; NZ_SWKA01000005.1.
DR PDB; 4ZLH; X-ray; 2.00 A; A/B=51-389.
DR PDBsum; 4ZLH; -.
DR AlphaFoldDB; P0AB60; -.
DR SMR; P0AB60; -.
DR STRING; 155864.EDL933_2410; -.
DR EnsemblBacteria; AAG56533; AAG56533; Z2526.
DR EnsemblBacteria; BAB35276; BAB35276; ECs_1853.
DR GeneID; 58460487; -.
DR GeneID; 912810; -.
DR KEGG; ece:Z2526; -.
DR KEGG; ecs:ECs_1853; -.
DR PATRIC; fig|386585.9.peg.1952; -.
DR eggNOG; COG2956; Bacteria.
DR HOGENOM; CLU_059365_1_0_6; -.
DR OMA; FWQCPGC; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Iron; Membrane;
KW Metal-binding; Reference proteome; Repeat; TPR repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..389
FT /note="Lipopolysaccharide assembly protein B"
FT /id="PRO_0000042575"
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"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 68..82
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 85..96
FT /evidence="ECO:0007829|PDB:4ZLH"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 103..120
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 123..131
FT /evidence="ECO:0007829|PDB:4ZLH"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:4ZLH"
FT TURN 137..139
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 157..168
FT /evidence="ECO:0007829|PDB:4ZLH"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 175..191
FT /evidence="ECO:0007829|PDB:4ZLH"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 197..209
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 214..226
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 240..243
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 245..251
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 252..261
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 282..311
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 315..328
FT /evidence="ECO:0007829|PDB:4ZLH"
FT HELIX 333..351
FT /evidence="ECO:0007829|PDB:4ZLH"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:4ZLH"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:4ZLH"
FT STRAND 363..366
FT /evidence="ECO:0007829|PDB:4ZLH"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:4ZLH"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:4ZLH"
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
