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Entry: A0A094IRQ6_9GAMM
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ID   A0A094IRQ6_9GAMM        Unreviewed;       385 AA.
AC   A0A094IRQ6;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-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=IDAT_01610 {ECO:0000313|EMBL:KFZ29817.1};
OS   Pseudidiomarina atlantica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Idiomarinaceae; Pseudidiomarina.
OX   NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ29817.1, ECO:0000313|Proteomes:UP000053718};
RN   [1] {ECO:0000313|EMBL:KFZ29817.1, ECO:0000313|Proteomes:UP000053718}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ29817.1,
RC   ECO:0000313|Proteomes:UP000053718};
RA   Du J., Lai Q., Shao Z.;
RT   "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
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:KFZ29817.1}.
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DR   EMBL; JPIN01000001; KFZ29817.1; -; Genomic_DNA.
DR   RefSeq; WP_034729607.1; NZ_JPIN01000001.1.
DR   AlphaFoldDB; A0A094IRQ6; -.
DR   STRING; 1517416.IDAT_01610; -.
DR   eggNOG; COG2956; Bacteria.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000053718; 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   SUPFAM; SSF81901; HCP-like; 2.
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}; 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        21..385
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   REPEAT          210..243
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          351..378
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         353
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         356
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         367
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         370
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ   SEQUENCE   385 AA;  43942 MW;  1617705A2896C973 CRC64;
     MLELLFLLLP VAAAYGWFMG RNSVRNEERR EQEEFSKQYV TGLNLLLSDQ PDKAVDLFIQ
     LLDVDSDTLE THWALGKLFR RRGEFDRAIK IHQNLTSRPA ISEQQRRHAM FELGLDYLAA
     GIFDRAEEML LALQTDKEFA EPCQRHLLEL YEATHEWDKA IKVALKLARI DANAQPVVAQ
     LYCELASLQD DPTITEKFYQ KARKHDPDNI RAALSLGRMW FEQGDYEKAQ RILKTIKDAD
     PAFISEALPT LQACYKAQGD EAGFVQYLHQ CVSEANSTSA AMLLSEAVAA AGTIEEAERF
     MQAALLRNPT MKGFHKLMDF HIRAADVGKA RDSLLMLQRL VQQQMQQRPK YRCRHCGFAG
     STLYWHCPSC RTWGEIKPIT GLDGD
//
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