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Database: UniProt
Entry: B7RYE5_9GAMM
LinkDB: B7RYE5_9GAMM
Original site: B7RYE5_9GAMM 
ID   B7RYE5_9GAMM            Unreviewed;       402 AA.
AC   B7RYE5;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN   ORFNames=GPB2148_1553 {ECO:0000313|EMBL:EEB78655.1};
OS   marine gamma proteobacterium HTCC2148.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae.
OX   NCBI_TaxID=247634 {ECO:0000313|EMBL:EEB78655.1, ECO:0000313|Proteomes:UP000002793};
RN   [1] {ECO:0000313|Proteomes:UP000002793}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2148 {ECO:0000313|Proteomes:UP000002793};
RX   PubMed=20472793; DOI=10.1128/jb.00511-10;
RA   Thrash J.C., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA   Giovannoni S.J.;
RT   "Genome sequences of strains HTCC2148 and HTCC2080, belonging to the
RT   OM60/NOR5 clade of the Gammaproteobacteria.";
RL   J. Bacteriol. 192:3842-3843(2010).
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}.
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DR   EMBL; DS999227; EEB78655.1; -; Genomic_DNA.
DR   AlphaFoldDB; B7RYE5; -.
DR   STRING; 247634.GPB2148_1553; -.
DR   eggNOG; COG2956; Bacteria.
DR   HOGENOM; CLU_059365_1_0_6; -.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000002793; 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   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR45586:SF17; LIPOPOLYSACCHARIDE ASSEMBLY PROTEIN B; 1.
DR   PANTHER; PTHR45586; TPR REPEAT-CONTAINING PROTEIN PA4667; 1.
DR   Pfam; PF18073; Rubredoxin_2; 1.
DR   Pfam; PF14559; TPR_19; 1.
DR   Pfam; PF13176; TPR_7; 1.
DR   SMART; SM00028; TPR; 4.
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:UP000002793};
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..21
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        22..402
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   DOMAIN          368..395
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         370
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         373
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         384
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         387
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ   SEQUENCE   402 AA;  45364 MW;  6039AED274AFAD4A CRC64;
     MNDYLVFALF FVAIVIGWYL GRRGQAKSAS APDLPGQYYK GLNYLLDGKP DGAVDAFINA
     LEVNSETLET HIALGNLLRK RGEVDRAIRI HQNLLARPSL PRAQVHQAHL ELARDYISAG
     LLDRAERLLL DLVAESPIQR RDSQLHLLDI YQSEREWQQA IDIAVELLPR KSLLGGTAGT
     AADEPGQSVP VILSHYYCEL AAERRQDNDL QGARQLLQEA LAMDKQSVRA SMMLGDVEFD
     AGRFKQAIKA LRRVRQQDPL YISESVPSLR ACYRELGDEK SLLAYVRECL DNHPSPPLLL
     AAAEDIREMD GGSTAEQFLI EQLDKMPSLR GMEKLVSFRI SASEDKPRED LNLLQQLVQR
     LIEQRPSYRC SHCGFAARQL HWFCPGCKYW GTIRPIRGTS ME
//
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