LPP20_HELPJ
ID LPP20_HELPJ Reviewed; 175 AA.
AC P0A0V1; P53436;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=LPP20 lipoprotein;
DE Flags: Precursor;
GN Name=lpp20; OrderedLocusNames=jhp_1349;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
CC -!- FUNCTION: Could play a role in the pathogenesis of H.pylori by serving
CC as an inflammatory mediator. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000255|PROSITE-ProRule:PRU00303}.
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DR EMBL; AE001439; AAD06926.1; -; Genomic_DNA.
DR PIR; H64701; H64701.
DR RefSeq; WP_000795978.1; NZ_CP011330.1.
DR PDB; 5OK8; X-ray; 1.87 A; A/B/C/D=1-175.
DR PDBsum; 5OK8; -.
DR AlphaFoldDB; P0A0V1; -.
DR SMR; P0A0V1; -.
DR STRING; 85963.jhp_1349; -.
DR EnsemblBacteria; AAD06926; AAD06926; jhp_1349.
DR KEGG; hpj:jhp_1349; -.
DR PATRIC; fig|85963.30.peg.1203; -.
DR OMA; NKEYSAQ; -.
DR Proteomes; UP000000804; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR002217; Lipo_LPP20.
DR InterPro; IPR024952; Lipo_LPP20-like.
DR Pfam; PF02169; LPP20; 1.
DR PIRSF; PIRSF011368; Lipo_LPP20; 1.
DR PRINTS; PR01019; LIPOLPP20.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 22..175
FT /note="LPP20 lipoprotein"
FT /id="PRO_0000018106"
FT LIPID 22
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 22
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT HELIX 46..49
FT /evidence="ECO:0007829|PDB:5OK8"
FT HELIX 52..55
FT /evidence="ECO:0007829|PDB:5OK8"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5OK8"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:5OK8"
FT HELIX 78..104
FT /evidence="ECO:0007829|PDB:5OK8"
FT HELIX 126..136
FT /evidence="ECO:0007829|PDB:5OK8"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:5OK8"
FT STRAND 141..147
FT /evidence="ECO:0007829|PDB:5OK8"
FT STRAND 149..159
FT /evidence="ECO:0007829|PDB:5OK8"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:5OK8"
SQ SEQUENCE 175 AA; 19108 MW; BBB8359E03C8458A CRC64;
MKNQVKKILG MSVVAAMVIV GCSHAPKSGI SKSNKAYKEA TKGAPDWVVG DLEKVAKYEK
YSGVFLGRAE DLITNNDVDY STNQATAKAR ANLAANLKST LQKDLENEKT RTVDASGKRS
ISGTDTEKIS QLVDKELIAS KMLARYVGKD RVFVLVGLDK QIVDKVREEL GMVKK
