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Database: UniProt
Entry: A0A1V4B0M9_9PAST
LinkDB: A0A1V4B0M9_9PAST
Original site: A0A1V4B0M9_9PAST 
ID   A0A1V4B0M9_9PAST        Unreviewed;       398 AA.
AC   A0A1V4B0M9;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN   ORFNames=NCTC1659_02130 {ECO:0000313|EMBL:STO60829.1};
OS   Canicola haemoglobinophilus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Canicola.
OX   NCBI_TaxID=733 {ECO:0000313|EMBL:STO60829.1, ECO:0000313|Proteomes:UP000254329};
RN   [1] {ECO:0000313|EMBL:STO60829.1, ECO:0000313|Proteomes:UP000254329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC1659 {ECO:0000313|EMBL:STO60829.1,
RC   ECO:0000313|Proteomes:UP000254329};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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}.
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DR   EMBL; UGHF01000001; STO60829.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4B0M9; -.
DR   STRING; 733.B0186_06835; -.
DR   OrthoDB; 507476at2; -.
DR   Proteomes; UP000254329; 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   Pfam; PF18073; Rubredoxin_2; 1.
DR   Pfam; PF13176; TPR_7; 1.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00994}; Reference proteome {ECO:0000313|Proteomes:UP000254329};
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        21..398
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   DOMAIN          364..391
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         366
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         369
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         380
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         383
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ   SEQUENCE   398 AA;  45566 MW;  2FFCBDE6F5E59B7E CRC64;
     MLELLFLLLP IAAAYGWYMG HRSARKDQDN ISNKLSRDYV AGVNLLLSNQ REKAADLFLD
     ILQKQEQENN IETGSQFEAE LTLGNLYRSR GEVDRALRIH QALDRSPNYT FEQKLLAKQQ
     LAKDFMAVGF YDRAESLYIL LVDEPNYAEG ALQQLTVIYQ KTKEWKKAIN VAEKLAKIAP
     QKNNTALAHY YCEYSLTLGS DEREQEQAIN LLQQALNVSK TSVRASLLIA ERYIVNLEYK
     SAVQNLENVL EQNADYVGEV LPALKYCYQE LNQLDNFELF LIRASQICRN SAVDLALSDL
     IAEKDGIMAA QSKLYQQLGQ NPSTFIFHRF IQYQIDTAEN GRAKDSLVLL HKMVGDRIAR
     GFSYRCSNCG YQTHKLLWNC PACQRWEKIK PITGIEHN
//
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