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Database: UniProt
Entry: D6H5M8_NEIGO
LinkDB: D6H5M8_NEIGO
Original site: D6H5M8_NEIGO 
ID   D6H5M8_NEIGO            Unreviewed;       402 AA.
AC   D6H5M8;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, 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=NGMG_02201 {ECO:0000313|EMBL:EFE05089.2};
OS   Neisseria gonorrhoeae DGI2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=528348 {ECO:0000313|EMBL:EFE05089.2, ECO:0000313|Proteomes:UP000002765};
RN   [1] {ECO:0000313|EMBL:EFE05089.2, ECO:0000313|Proteomes:UP000002765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DGI2 {ECO:0000313|EMBL:EFE05089.2,
RC   ECO:0000313|Proteomes:UP000002765};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Yandava C.,
RA   Gujja S., Alvarado L., Berlin A., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Heiman D., Hepburn T.,
RA   Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M.,
RA   Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA   Walk T., White J., Rice P., Seifert H., Lander E., Nusbaum C., Galagan J.,
RA   Birren B.;
RT   "The Genome Sequence of Neisseria gonorrhoeae DGI2.";
RL   Submitted (MAR-2009) 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; GG749023; EFE05089.2; -; Genomic_DNA.
DR   AlphaFoldDB; D6H5M8; -.
DR   Proteomes; UP000002765; 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; PF13432; TPR_16; 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, ECO:0000256|SAM:Phobius};
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, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_00994,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        40..402
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   DOMAIN          370..397
FT                   /note="LapB rubredoxin metal binding"
FT                   /evidence="ECO:0000259|Pfam:PF18073"
FT   BINDING         372
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         375
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         386
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   BINDING         389
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
SQ   SEQUENCE   402 AA;  45926 MW;  710927AACA7E8A7F CRC64;
     MLPNLPNSLK KADMDNELWI ILLPIILLPV FFTMGWFAAR VDMKTVLKQA KSIPSGFYKS
     LDALVDRNSG RAARELAEVV DGRPQSYDLN LTLGKLYRQR GENDKAINIH RTMLDSPDTV
     GEKRARVLFE LAQNYQSAGL VDRAEQIFLG LQDGEMAREA RQHLLNIYQQ DRDWEKAVET
     AQLLSHDEQT YQFEIAQFYC ELAQAALFKS NFDAARFNVG KALEANKKCT RANMILGDIE
     HRQGNFPAAV EAYAAIEQQN HAYLSMVGEK LYEAYAAQGK PEEGLNRLTG YMQTFPELDL
     INVVYEKSLL LKGEKEAAQT AVELVRRKPD LNGVYRLLGL KLSDLDPAWK ADADMMRSVI
     GRQLQRSVMY RCRNCHFKSQ VFFWHCPACN KWQTFTPNKI EV
//
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