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Database: UniProt
Entry: B7L4B6_ECO55
LinkDB: B7L4B6_ECO55
Original site: B7L4B6_ECO55 
ID   B7L4B6_ECO55            Unreviewed;       389 AA.
AC   B7L4B6;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=Lipopolysaccharide assembly protein B {ECO:0000256|HAMAP-Rule:MF_00994};
GN   Name=yciM {ECO:0000313|EMBL:CAU97299.1};
GN   Synonyms=lapB {ECO:0000256|HAMAP-Rule:MF_00994};
GN   OrderedLocusNames=EC55989_1441 {ECO:0000313|EMBL:CAU97299.1};
OS   Escherichia coli (strain 55989 / EAEC).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585055 {ECO:0000313|EMBL:CAU97299.1, ECO:0000313|Proteomes:UP000000746};
RN   [1] {ECO:0000313|Proteomes:UP000000746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=55989 / EAEC {ECO:0000313|Proteomes:UP000000746};
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928145; CAU97299.1; -; Genomic_DNA.
DR   RefSeq; WP_000891353.1; NC_011748.1.
DR   AlphaFoldDB; B7L4B6; -.
DR   SMR; B7L4B6; -.
DR   GeneID; 75203393; -.
DR   KEGG; eck:EC55989_1441; -.
DR   HOGENOM; CLU_059365_1_0_6; -.
DR   OMA; FWQCPGC; -.
DR   Proteomes; UP000000746; Chromosome.
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:SF1; 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; 5.
DR   SUPFAM; SSF48452; TPR-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}; Reference proteome {ECO:0000313|Proteomes:UP000000746};
KW   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..389
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00994"
FT   REPEAT          214..247
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
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;  44531 MW;  F4D1B9E2A526BCC3 CRC64;
     MLELLFLLLP VAAAYGWYMG RRSAQQNKQD EANRLSRDYV AGVNFLLSNQ QDKAVDLFLD
     MLKEDTGTVE AHLTLGNLFR SRGEVDRAIR IHQTLMESAS LTYEQRLLAI QQLGRDYMAA
     GLYDRAEDMF NQLTDETDFR IGALQQLLQI YQATSEWQKA IDVAERLVKL GKDKQRVEIA
     HFYCELALQH MASDDLDRAM TLLKKGAAAD KNSARVSIMM GRVFMAKGEY AKAVESLQRV
     ISQDRELVSE TLEMLQTCYQ QLGKTAEWAE FLQRAVEENT GADAELMLAD IIEARDGSEA
     AQVYITRQLQ RHPTMRVFHK LMDYHLNEAE EGRAKESLMV LRDMVGEKVR SKPRYRCQKC
     GFTAYTLYWH CPSCRAWSTI KPIRGLDGL
//
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