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Database: UniProt
Entry: A0A091AYW2_9GAMM
LinkDB: A0A091AYW2_9GAMM
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ID   A0A091AYW2_9GAMM        Unreviewed;       392 AA.
AC   A0A091AYW2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN   ORFNames=N789_00130 {ECO:0000313|EMBL:KFN44447.1};
OS   Arenimonas oryziterrae DSM 21050 = YC6267.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Arenimonas.
OX   NCBI_TaxID=1121015 {ECO:0000313|EMBL:KFN44447.1, ECO:0000313|Proteomes:UP000029385};
RN   [1] {ECO:0000313|EMBL:KFN44447.1, ECO:0000313|Proteomes:UP000029385}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YC6267 {ECO:0000313|EMBL:KFN44447.1,
RC   ECO:0000313|Proteomes:UP000029385};
RA   Chen F., Wang G.;
RT   "Genome sequencing of Arenimonas oryziterrae.";
RL   Submitted (SEP-2013) 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:KFN44447.1}.
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DR   EMBL; AVCI01000001; KFN44447.1; -; Genomic_DNA.
DR   RefSeq; WP_022968619.1; NZ_AVCI01000001.1.
DR   AlphaFoldDB; A0A091AYW2; -.
DR   STRING; 1121015.GCA_000420545_00973; -.
DR   PATRIC; fig|1121015.4.peg.27; -.
DR   eggNOG; COG2956; Bacteria.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000029385; 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; 3.
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; PF13432; TPR_16; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   Pfam; PF13176; TPR_7; 1.
DR   SUPFAM; SSF48452; TPR-like; 2.
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:UP000029385};
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};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994}.
FT   TOPO_DOM        25..392
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   DOMAIN          358..385
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         360
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         363
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"
FT   BINDING         377
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ   SEQUENCE   392 AA;  43545 MW;  1AA8D3FAA49C3190 CRC64;
     MAIMTHAAWL LLIPAAAAGG WLAGRRGGEI KGGARVSRLS NTYFRGLNYL LNEQQDKAIE
     IFLQIAEVDK DTIETQFALG HLFRRRGEVD RAIRLHQGLV ARNGLSEEQK TRAVLALGED
     YMRAGLLDRA ETLFTDLVQM GVHAPQALRQ LIAIYQAERD WDKAIEHATR YEQTSGEPMG
     RVIAHFHCEL ADKARLEGRV DVAREQIGLA YSADSNSVRA GVIEGRLELA EGNDAGAIRA
     FERVARHDIE YLPEILSSLL SCYEKRGEIA RARGFLQEVI EHYPGVSPVL ALAQIIQRDE
     GIGVAQAFLA RQLQQRPSVR GEAALIDLSL ENPGDDPAES LRVIKQITDQ LVVRTMSYRC
     QRCGFGARAH HWQCPSCKHW GSIKPQLNAA GD
//
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