ID A0A2G0Q4Z1_9GAMM Unreviewed; 389 AA.
AC A0A2G0Q4Z1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN ORFNames=Xhom_03339 {ECO:0000313|EMBL:PHM54262.1};
OS Xenorhabdus hominickii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351679 {ECO:0000313|EMBL:PHM54262.1, ECO:0000313|Proteomes:UP000225433};
RN [1] {ECO:0000313|EMBL:PHM54262.1, ECO:0000313|Proteomes:UP000225433}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17903 {ECO:0000313|EMBL:PHM54262.1,
RC ECO:0000313|Proteomes:UP000225433};
RX PubMed=28993611; DOI=10.1038/s41564-017-0039-9;
RA Tobias N.J., Wolff H., Djahanschiri B., Grundmann F., Kronenwerth M.,
RA Shi Y.M., Simonyi S., Grun P., Shapiro-Ilan D., Pidot S.J., Stinear T.P.,
RA Ebersberger I., Bode H.B.;
RT "Natural product diversity associated with the nematode symbionts
RT Photorhabdus and Xenorhabdus.";
RL Nat. Microbiol. 2:1676-1685(2017).
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:PHM54262.1}.
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DR EMBL; NJAI01000005; PHM54262.1; -; Genomic_DNA.
DR RefSeq; WP_069315841.1; NZ_NJAI01000005.1.
DR AlphaFoldDB; A0A2G0Q4Z1; -.
DR STRING; 351679.A9255_05625; -.
DR KEGG; xho:A9255_05625; -.
DR OrthoDB; 507476at2; -.
DR Proteomes; UP000225433; 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; 1.
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; 3.
DR SUPFAM; SSF81901; HCP-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};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00994}; Repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW TPR repeat {ECO:0000256|HAMAP-Rule:MF_00994};
KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_00994};
KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994}.
FT TOPO_DOM 21..389
FT /note="Cytoplasmic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT DOMAIN 355..382
FT /note="LapB rubredoxin metal binding"
FT /evidence="ECO:0000259|Pfam:PF18073"
FT BINDING 357
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 360
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 371
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT BINDING 374
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ SEQUENCE 389 AA; 44908 MW; 9F76864A64AB62B2 CRC64;
MLELLFLLLP IAAAYGWYMG RRSAQQDKQQ SADRLSRGYV DGVNFLLSNQ QDKAVDLFLD
MLKEDSSAFE AHLTLGNLFR SRGEVERAIR IHQSLMESAS LTFEQRLLAI QQLGRDYMAA
GVYDRAENMF LQLIDETDFR ENALNSLLTI YQSTSDWSKT IEVAEKLVKL GKPHFREEIA
HFYCELALQC MGRDDFSEAI GYLNKAAQAD KNCARVSIML GRIYISQGEY AKAVGTLKCV
LEQDKQLISE SLPMLQECYQ RLSQPKEWET FVQCCVEEKC GAISELHMAD IIERNEGRDI
AQNYINRQLE RHPTMRLFYR LMDYHLVDAE EGRAKESLIL LRNMVGEQIR TKPDYRCHKC
GFTSRSLYWH CPSCRSWDSI KPIRGLDGQ
//
