BLC_ECOLI
ID BLC_ECOLI Reviewed; 177 AA.
AC P0A901; P39281; Q2M6F3;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Outer membrane lipoprotein Blc;
DE Flags: Precursor;
GN Name=blc; Synonyms=yjeL; OrderedLocusNames=b4149, JW4110;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / CS520;
RX PubMed=7559452; DOI=10.1074/jbc.270.39.23097;
RA Bishop R.E., Penfold S.S., Frost L.S., Hoeltje J.-V., Weiner J.H.;
RT "Stationary phase expression of a novel Escherichia coli outer membrane
RT lipoprotein and its relationship with mammalian apolipoprotein D.
RT Implications for the origin of lipocalins.";
RL J. Biol. Chem. 270:23097-23103(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 23-177, AND FUNCTION.
RX PubMed=15044022; DOI=10.1016/s0014-5793(04)00199-1;
RA Campanacci V., Nurizzo D., Spinelli S., Valencia C., Tegoni M.,
RA Cambillau C.;
RT "The crystal structure of the Escherichia coli lipocalin Blc suggests a
RT possible role in phospholipid binding.";
RL FEBS Lett. 562:183-188(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 23-177 IN COMPLEX WITH VACCENIC
RP ACID, SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=16920109; DOI=10.1016/j.febslet.2006.07.086;
RA Campanacci V., Bishop R.E., Blangy S., Tegoni M., Cambillau C.;
RT "The membrane bound bacterial lipocalin Blc is a functional dimer with
RT binding preference for lysophospholipids.";
RL FEBS Lett. 580:4877-4883(2006).
CC -!- FUNCTION: Involved in the storage or transport of lipids necessary for
CC membrane maintenance under stressful conditions. Displays a binding
CC preference for lysophospholipids. {ECO:0000269|PubMed:15044022}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16920109}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Lipid-anchor.
CC -!- INDUCTION: By starvation and high osmolarity.
CC -!- SIMILARITY: Belongs to the calycin superfamily. Lipocalin family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U21726; AAC46452.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97048.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77109.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78153.1; -; Genomic_DNA.
DR PIR; I84534; I84534.
DR RefSeq; NP_418573.1; NC_000913.3.
DR RefSeq; WP_001238378.1; NZ_LN832404.1.
DR PDB; 1QWD; X-ray; 1.75 A; A/B=23-177.
DR PDB; 2ACO; X-ray; 1.80 A; A/B=23-177.
DR PDB; 3MBT; X-ray; 2.60 A; A=19-177.
DR PDB; 6UKK; X-ray; 1.60 A; A=23-177.
DR PDBsum; 1QWD; -.
DR PDBsum; 2ACO; -.
DR PDBsum; 3MBT; -.
DR PDBsum; 6UKK; -.
DR AlphaFoldDB; P0A901; -.
DR SMR; P0A901; -.
DR BioGRID; 4261278; 195.
DR DIP; DIP-35862N; -.
DR IntAct; P0A901; 6.
DR STRING; 511145.b4149; -.
DR jPOST; P0A901; -.
DR PaxDb; P0A901; -.
DR PRIDE; P0A901; -.
DR EnsemblBacteria; AAC77109; AAC77109; b4149.
DR EnsemblBacteria; BAE78153; BAE78153; BAE78153.
DR GeneID; 66671937; -.
DR GeneID; 948670; -.
DR KEGG; ecj:JW4110; -.
DR KEGG; eco:b4149; -.
DR PATRIC; fig|1411691.4.peg.2549; -.
DR EchoBASE; EB2367; -.
DR eggNOG; COG3040; Bacteria.
DR HOGENOM; CLU_068449_3_0_6; -.
DR InParanoid; P0A901; -.
DR OMA; YSCTTIV; -.
DR PhylomeDB; P0A901; -.
DR BioCyc; EcoCyc:G7837-MON; -.
DR EvolutionaryTrace; P0A901; -.
DR PRO; PR:P0A901; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006629; P:lipid metabolic process; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; IBA:GO_Central.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR022271; Lipocalin_ApoD.
DR InterPro; IPR002446; Lipocalin_bac.
DR InterPro; IPR022272; Lipocalin_CS.
DR InterPro; IPR000566; Lipocln_cytosolic_FA-bd_dom.
DR Pfam; PF08212; Lipocalin_2; 1.
DR PIRSF; PIRSF036893; Lipocalin_ApoD; 1.
DR PRINTS; PR01171; BCTLIPOCALIN.
DR SUPFAM; SSF50814; SSF50814; 1.
DR PROSITE; PS00213; LIPOCALIN; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipid-binding; Lipoprotein; Membrane;
KW Palmitate; Reference proteome; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000305"
FT CHAIN 19..177
FT /note="Outer membrane lipoprotein Blc"
FT /id="PRO_0000017991"
FT LIPID 19
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000305"
FT LIPID 19
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000305"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:1QWD"
FT HELIX 36..39
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:6UKK"
FT TURN 52..56
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 58..66
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 72..80
FT /evidence="ECO:0007829|PDB:6UKK"
FT TURN 81..84
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 85..97
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 104..108
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 127..131
FT /evidence="ECO:0007829|PDB:6UKK"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:6UKK"
FT HELIX 149..161
FT /evidence="ECO:0007829|PDB:6UKK"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:6UKK"
SQ SEQUENCE 177 AA; 19852 MW; BFF9A53A099B0048 CRC64;
MRLLPLVAAA TAAFLVVACS SPTPPRGVTV VNNFDAKRYL GTWYEIARFD HRFERGLEKV
TATYSLRDDG GLNVINKGYN PDRGMWQQSE GKAYFTGAPT RAALKVSFFG PFYGGYNVIA
LDREYRHALV CGPDRDYLWI LSRTPTISDE VKQEMLAVAT REGFDVSKFI WVQQPGS
