ID   BMPD_BORBJ              Reviewed;         341 AA.
AC   E4S1L1; Q44743;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   08-FEB-2011, sequence version 1.
DT   25-MAY-2022, entry version 45.
DE   RecName: Full=Basic membrane protein D;
DE   Flags: Precursor;
GN   Name=bmpD; OrderedLocusNames=BbuJD1_0385;
OS   Borreliella burgdorferi (strain JD1) (Borrelia burgdorferi).
OC   Bacteria; Spirochaetes; Spirochaetales; Borreliaceae; Borreliella.
OX   NCBI_TaxID=521008;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=JD1;
RX   PubMed=8606088; DOI=10.1128/iai.64.4.1259-1264.1996;
RA   Ramamoorthy R., Povinelli L., Philipp M.T.;
RT   "Molecular characterization, genomic arrangement, and expression of bmpD, a
RT   new member of the bmp class of genes encoding membrane proteins of Borrelia
RT   burgdorferi.";
RL   Infect. Immun. 64:1259-1264(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JD1;
RX   PubMed=20935092; DOI=10.1128/jb.01158-10;
RA   Schutzer S.E., Fraser-Liggett C.M., Casjens S.R., Qiu W.G., Dunn J.J.,
RA   Mongodin E.F., Luft B.J.;
RT   "Whole-genome sequences of thirteen isolates of Borrelia burgdorferi.";
RL   J. Bacteriol. 193:1018-1020(2011).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the BMP lipoprotein family. {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; U35450; AAC43984.1; -; Genomic_DNA.
DR   EMBL; CP002312; ADQ30731.1; -; Genomic_DNA.
DR   RefSeq; WP_002656205.1; NC_017403.1.
DR   PDB; 6SHU; X-ray; 1.43 A; A=18-341.
DR   PDBsum; 6SHU; -.
DR   AlphaFoldDB; E4S1L1; -.
DR   SMR; E4S1L1; -.
DR   GeneID; 56567813; -.
DR   KEGG; bbj:BbuJD1_0385; -.
DR   PATRIC; fig|521008.3.peg.644; -.
DR   HOGENOM; CLU_038813_0_0_12; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR028082; Peripla_BP_I.
DR   InterPro; IPR003760; PnrA-like.
DR   Pfam; PF02608; Bmp; 1.
DR   SUPFAM; SSF53822; SSF53822; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate; Signal.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000305"
FT   CHAIN           17..341
FT                   /note="Basic membrane protein D"
FT                   /id="PRO_0000406193"
FT   LIPID           17
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000305"
FT   LIPID           17
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000305"
FT   STRAND          29..36
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          40..42
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           43..58
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          61..67
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           72..81
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          85..91
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           92..94
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           95..104
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          110..114
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          126..131
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           133..147
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          149..159
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           162..178
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          183..188
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          190..193
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           195..207
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          212..217
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           219..231
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          236..242
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   TURN            249..251
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          252..258
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           260..274
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          280..285
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   TURN            287..290
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   STRAND          291..296
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           298..300
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           301..319
FT                   /evidence="ECO:0007829|PDB:6SHU"
FT   HELIX           329..337
FT                   /evidence="ECO:0007829|PDB:6SHU"
SQ   SEQUENCE   341 AA;  37163 MW;  63FF6638F81A91D5 CRC64;
     MLKKVYYFLI FLFIVACSSS DDGKSEAKTV SLIVDGAFDD KGFNESSSKA IRKLKADLNI
     NIIEKASTGN SYLGDIANLE DGNSNLIWGI GFRLSDILFQ RASENVSVNY AIIEGVYDEI
     QIPKNLLNIS FRSEEVAFLA GYFASKASKT GKIGFVGGVR GKVLESFMYG YEAGAKYANS
     NIKVVSQYVG TFGDFGLGRS TASNMYRDGV DIIFAAAGLS GIGVIEAAKE LGPDHYIIGV
     DQDQSYLAPN NVIVSAVKKV DSLMYSLTKK YLETGVLDGG KTMFLGLKED GLGLVLNENL
     KSNYSEIYNK SLKIGQSIMN GIIKVPYDKV SYDNFVLQME N