ID E7RTM4_9BURK Unreviewed; 394 AA.
AC E7RTM4;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 49.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN ORFNames=HMPREF0551_0293 {ECO:0000313|EMBL:EFV96110.1};
OS Lautropia mirabilis ATCC 51599.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Lautropia.
OX NCBI_TaxID=887898 {ECO:0000313|EMBL:EFV96110.1, ECO:0000313|Proteomes:UP000011021};
RN [1] {ECO:0000313|EMBL:EFV96110.1, ECO:0000313|Proteomes:UP000011021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51599 {ECO:0000313|EMBL:EFV96110.1,
RC ECO:0000313|Proteomes:UP000011021};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (DEC-2010) 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:EFV96110.1}.
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DR EMBL; AEQP01000001; EFV96110.1; -; Genomic_DNA.
DR RefSeq; WP_005672145.1; NZ_GL636062.1.
DR AlphaFoldDB; E7RTM4; -.
DR STRING; 887898.HMPREF0551_0293; -.
DR eggNOG; COG2956; Bacteria.
DR HOGENOM; CLU_059365_1_0_4; -.
DR Proteomes; UP000011021; 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 Pfam; PF18073; Rubredoxin_2; 1.
DR Pfam; PF13432; TPR_16; 2.
DR SUPFAM; SSF48452; TPR-like; 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, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00994}; Reference proteome {ECO:0000313|Proteomes:UP000011021};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW TPR repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00994, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..22
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TOPO_DOM 23..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT DOMAIN 359..383
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
FT BINDING 361
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 364
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 375
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 378
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ SEQUENCE 394 AA; 44104 MW; 1C10AD892EEDD399 CRC64;
MEFEYWWLLA IPLAFGLGWV ASRREGRLDE RPATMGNAYF RGVNLLLNEQ SDKAIDAFVD
VVRIEPEASE LHFALGSLFR RRGETDRAIR VHQNLVDRPD LDDRTRAHAL YELGLDFLKA
GLVDRAEDSF NRLQGTEYAE AASRQRLEIA QRSHDWERVV DLARATPAEP GFDPKLIIAQ
ASCELAMAAL RARQFDKAHQ FVEQAQQALP DHPRPLVVEG EIALAEGQPA AAIEAWTRLA
DKHPEQVERV VDHWLKAADA VGGDEGVRLA IARLQQLDVA QAPEMLRAMS EAISRLDGKA
AAAQWVRQLV NKHPTLSGLQ VLLSLSRRGD KNGPATVEDL DEDALAATLR KLTQRMSHYG
CRVCGFRGQQ YYWQCPGCGR WDSYGPRPGE ESVS
//