ID TPN32_TREPA Reviewed; 268 AA.
AC O07950;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Membrane lipoprotein TpN32;
DE AltName: Full=29 kDa protein;
DE Flags: Precursor;
GN Name=tpn32; OrderedLocusNames=TP_0821;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Treponemataceae;
OC Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Porcella S.F., Radolf J.D., Norgard M.V.;
RT "Treponema pallidum 29K protein is homologous to a lipoprotein present in
RT Pasteurella hemolytica and in Haemophilus influenzae type b.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RA Stamm L.V., Barnes N.Y.;
RT "Treponema pallidum lipoprotein homologue.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the NlpA lipoprotein family. {ECO:0000305}.
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DR EMBL; U97358; AAB63362.1; -; Genomic_DNA.
DR EMBL; U93844; AAB61267.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65789.1; -; Genomic_DNA.
DR PIR; G71275; G71275.
DR RefSeq; WP_010882265.1; NC_021490.2.
DR PDB; 1XS5; X-ray; 1.85 A; A=28-268.
DR PDBsum; 1XS5; -.
DR AlphaFoldDB; O07950; -.
DR SMR; O07950; -.
DR STRING; 243276.TP_0821; -.
DR EnsemblBacteria; AAC65789; AAC65789; TP_0821.
DR GeneID; 57879338; -.
DR KEGG; tpa:TP_0821; -.
DR eggNOG; COG1464; Bacteria.
DR HOGENOM; CLU_067080_0_0_12; -.
DR OrthoDB; 9812878at2; -.
DR EvolutionaryTrace; O07950; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR CDD; cd13597; PBP2_lipoprotein_Tp32; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR InterPro; IPR004872; Lipoprotein_NlpA.
DR PANTHER; PTHR30429; D-METHIONINE-BINDING LIPOPROTEIN METQ; 1.
DR PANTHER; PTHR30429:SF0; METHIONINE-BINDING LIPOPROTEIN METQ; 1.
DR Pfam; PF03180; Lipoprotein_9; 1.
DR PIRSF; PIRSF002854; MetQ; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 24..268
FT /note="Membrane lipoprotein TpN32"
FT /id="PRO_0000019750"
FT LIPID 24
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 24
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 41..53
FT /evidence="ECO:0007829|PDB:1XS5"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 67..75
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 78..86
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 137..149
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 168..170
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 199..204
FT /evidence="ECO:0007829|PDB:1XS5"
FT TURN 209..212
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:1XS5"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:1XS5"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:1XS5"
SQ SEQUENCE 268 AA; 29081 MW; AB21F8A07A88F691 CRC64;
MKGKTVSAAL VGKLIALSVG VVACTQVKDE TVGVGVLSEP HARLLEIAKE EVKKQHIELR
IVEFTNYVAL NEAVMRGDIL MNFFQHVPHM QQFNQEHNGD LVSVGNVHVE PLALYSRTYR
HVSDFPAGAV IAIPNDSSNE ARALRLLEAA GFIRMRAGSG LFATVEDVQQ NVRNVVLQEV
ESALLPRVFD QVDGAVINGN YAIMAGLSAR RDGLAVEPDA SAYANVLVVK RGNEADARVQ
AVLRALCGGR VRTYLKERYK GGEVAPAL
//
