ID A0A081NH29_9GAMM Unreviewed; 391 AA.
AC A0A081NH29;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN ORFNames=GZ78_08710 {ECO:0000313|EMBL:KEQ17752.1};
OS Endozoicomonas numazuensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Endozoicomonadaceae; Endozoicomonas.
OX NCBI_TaxID=1137799 {ECO:0000313|EMBL:KEQ17752.1, ECO:0000313|Proteomes:UP000028073};
RN [1] {ECO:0000313|EMBL:KEQ17752.1, ECO:0000313|Proteomes:UP000028073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25634 {ECO:0000313|EMBL:KEQ17752.1,
RC ECO:0000313|Proteomes:UP000028073};
RA Neave M.J., Apprill A., Voolstra C.R.;
RT "Whole Genome Sequences of Three Symbiotic Endozoicomonas Bacteria.";
RL Submitted (JUN-2014) 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:KEQ17752.1}.
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DR EMBL; JOKH01000002; KEQ17752.1; -; Genomic_DNA.
DR RefSeq; WP_034834622.1; NZ_JOKH01000002.1.
DR AlphaFoldDB; A0A081NH29; -.
DR STRING; 1137799.GZ78_08710; -.
DR eggNOG; COG2956; Bacteria.
DR OrthoDB; 507476at2; -.
DR Proteomes; UP000028073; 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; IPR031636; PknG_TPR.
DR InterPro; IPR041166; Rubredoxin_2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF16918; PknG_TPR; 1.
DR Pfam; PF18073; Rubredoxin_2; 1.
DR Pfam; PF13176; TPR_7; 1.
DR SMART; SM00028; TPR; 4.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00994}; Reference proteome {ECO:0000313|Proteomes:UP000028073};
KW Repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW TPR repeat {ECO:0000256|HAMAP-Rule:MF_00994, ECO:0000256|PROSITE-
KW ProRule:PRU00339}; Transmembrane {ECO:0000256|HAMAP-Rule:MF_00994};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994}.
FT TOPO_DOM 22..391
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT REPEAT 37..70
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 105..255
FT /note="Protein kinase G tetratricopeptide repeat
FT containing"
FT /evidence="ECO:0000259|Pfam:PF16918"
FT DOMAIN 357..384
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
FT BINDING 359
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 362
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 376
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ SEQUENCE 391 AA; 44523 MW; 664C492B62872830 CRC64;
MPDLALLALI MVAMLAGYLL GRAEKKKKKE HFPEQPLSKE YFVGLNYLLN EQTDEAIETF
IKALDLNNDT VDTYLALGSL FCRRGEVDKS IRVHQDLLAR PSLTPLQSIR VQLELAKDYM
TAGLFDRAEA MLVDLSRQNH EYRVDALQQL LRIYEREKEW PQAVEITESL RKLCGEDYAP
RLAHLYCEIA EDKLRLNDRS GARKYIRAAY SRDKNCVRAS LILGRMEMEE GRDRDAIKAL
QKVSYQDNRY VPLTLDMLET VCHRSDQQRA LGSYLAKCLN EKPGTAIILA MTAQLMNSRG
EVSAMDFLTG QLRRQPSLRG LNALMNIQLN YPSEPSLTSI KLLKEVTDQM LVSKPVYQCF
SCGFAGKEMH WHCPGCHEWG TLAPVQGVEG E
//