ID   BLC_VIBCH               Reviewed;         171 AA.
AC   Q08790; O31025; O31027; Q9KML7;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 2.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Outer membrane lipoprotein Blc;
DE   AltName: Full=Protein Vlp;
DE   Flags: Precursor;
GN   Name=blc; Synonyms=vlp, vlpA; OrderedLocusNames=VC_A0317;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1;
RX   PubMed=8514410; DOI=10.1128/iai.61.7.3032-3037.1993;
RA   Franzon V.L., Barker A., Manning P.A.;
RT   "Nucleotide sequence encoding the mannose-fucose-resistant hemagglutinin of
RT   Vibrio cholerae O1 and construction of a mutant.";
RL   Infect. Immun. 61:3032-3037(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 25870 / Classical Inaba 569B / Serotype O1, and
RC   El Tor O17 / Serotype O1;
RA   Kaewrakon P., Manning P.A.;
RL   Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000250}; Lipid-anchor
CC       {ECO:0000250}.
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; X64097; CAA45443.1; -; Genomic_DNA.
DR   EMBL; AF025662; AAB81982.1; -; Genomic_DNA.
DR   EMBL; AF025663; AAB81984.1; -; Genomic_DNA.
DR   EMBL; AE003853; AAF96225.1; -; Genomic_DNA.
DR   PIR; G82474; G82474.
DR   PIR; S37731; S37731.
DR   RefSeq; NP_232713.1; NC_002506.1.
DR   RefSeq; WP_001201520.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q08790; -.
DR   SMR; Q08790; -.
DR   STRING; 243277.VC_A0317; -.
DR   DNASU; 2612408; -.
DR   EnsemblBacteria; AAF96225; AAF96225; VC_A0317.
DR   KEGG; vch:VC_A0317; -.
DR   PATRIC; fig|243277.26.peg.2952; -.
DR   eggNOG; COG3040; Bacteria.
DR   HOGENOM; CLU_068449_3_0_6; -.
DR   OMA; YSCTTIV; -.
DR   BioCyc; VCHO:VCA0317-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
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: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.
PE   3: Inferred from homology;
KW   Cell outer membrane; Lipid-binding; Lipoprotein; Membrane; Palmitate;
KW   Reference proteome; Signal.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000305"
FT   CHAIN           16..171
FT                   /note="Outer membrane lipoprotein Blc"
FT                   /id="PRO_0000017993"
FT   LIPID           16
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           16
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   VARIANT         10
FT                   /note="S -> A (in strain: N16961)"
FT   VARIANT         68
FT                   /note="S -> L (in strain: O17)"
FT   CONFLICT        50
FT                   /note="R -> K (in Ref. 2; AAB81982/AAB81984)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        170
FT                   /note="Q -> L (in Ref. 1; CAA45443)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   171 AA;  19686 MW;  447629EE5F9F5306 CRC64;
     MRAIFLILCS VLLNGCLGMP ESVKPVSDFE LNNYLGKWYE VARLDHSFER GLSQVTAEYR
     VRNDGGISVL NRGYSEEKGE WKEAEGKAYF VNGSTDGYLK VSFFGPFYGS YVVFELDREN
     YSYAFVSGPN TEYLWLLSRT PTVERGILDK FIEMSKERGF DTNRLIYVQQ Q