TP453_TREPA
ID TP453_TREPA Reviewed; 287 AA.
AC O67998; F7IW75; Q7DFP5;
DT 09-DEC-2015, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=Outer membrane protein TP0453 {ECO:0000303|PubMed:16159783};
DE AltName: Full=30kLP {ECO:0000303|Ref.1};
DE Flags: Precursor;
GN OrderedLocusNames=TP_0453; ORFNames=TPANIC_0453;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols-Farmington;
RA Shevchenko D.V., Akins D.R., Robinson E.J., Shevchenko O.V., Radolf J.D.;
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=24058545; DOI=10.1371/journal.pone.0074319;
RA Petrosova H., Pospisilova P., Strouhal M., Cejkova D., Zobanikova M.,
RA Mikalova L., Sodergren E., Weinstock G.M., Smajs D.;
RT "Resequencing of Treponema pallidum ssp. pallidum strains Nichols and SS14:
RT correction of sequencing errors resulted in increased separation of
RT syphilis treponeme subclusters.";
RL PLoS ONE 8:E74319-E74319(2013).
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=12904373; DOI=10.1128/jcm.41.8.3668-3674.2003;
RA Van Voorhis W.C., Barrett L.K., Lukehart S.A., Schmidt B., Schriefer M.,
RA Cameron C.E.;
RT "Serodiagnosis of syphilis: antibodies to recombinant Tp0453, Tp92, and Gpd
RT proteins are sensitive and specific indicators of infection by Treponema
RT pallidum.";
RL J. Clin. Microbiol. 41:3668-3674(2003).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DOMAIN, PALMITOYLATION,
RP MUTAGENESIS OF ILE-277, AND EXPRESSION IN E.COLI.
RC STRAIN=Nichols-Farmington;
RX PubMed=16159783; DOI=10.1128/jb.187.18.6499-6508.2005;
RA Hazlett K.R., Cox D.L., Decaffmeyer M., Bennett M.P., Desrosiers D.C.,
RA La Vake C.J., La Vake M.E., Bourell K.W., Robinson E.J., Brasseur R.,
RA Radolf J.D.;
RT "TP0453, a concealed outer membrane protein of Treponema pallidum, enhances
RT membrane permeability.";
RL J. Bacteriol. 187:6499-6508(2005).
RN [6]
RP BIOTECHNOLOGY.
RC STRAIN=Nichols;
RX PubMed=23100335; DOI=10.1128/jcm.01390-12;
RA Smith B.C., Simpson Y., Morshed M.G., Cowen L.L., Hof R., Wetherell C.,
RA Cameron C.E.;
RT "New proteins for a new perspective on syphilis diagnosis.";
RL J. Clin. Microbiol. 51:105-111(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 27-287, FUNCTION, SUBUNIT,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF ILE-62; LEU-162; LEU-201;
RP VAL-249 AND ILE-277.
RC STRAIN=Nichols-Farmington;
RX PubMed=21965687; DOI=10.1074/jbc.m111.305284;
RA Luthra A., Zhu G., Desrosiers D.C., Eggers C.H., Mulay V., Anand A.,
RA McArthur F.A., Romano F.B., Caimano M.J., Heuck A.P., Malkowski M.G.,
RA Radolf J.D.;
RT "The transition from closed to open conformation of Treponema pallidum
RT outer membrane-associated lipoprotein TP0453 involves membrane sensing and
RT integration by two amphipathic helices.";
RL J. Biol. Chem. 286:41656-41668(2011).
CC -!- FUNCTION: Might be involved in ligand transport, alters membrane
CC permeability at acidic pH (4.0 to 5.5) (PubMed:21965687). Incubation of
CC the non-lipidated form with lipid vesicles increases their permeability
CC (PubMed:16159783). {ECO:0000269|PubMed:16159783,
CC ECO:0000269|PubMed:21965687}.
CC -!- SUBUNIT: A mix of monomer and dimers; may integrate into the membrane
CC as a dimer. {ECO:0000269|PubMed:21965687, ECO:0000305|PubMed:16159783}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000269|PubMed:16159783,
CC ECO:0000305|PubMed:21965687}; Lipid-anchor {ECO:0000255|PROSITE-
CC ProRule:PRU00303, ECO:0000305|PubMed:16159783}; Periplasmic side
CC {ECO:0000305|PubMed:16159783, ECO:0000305|PubMed:21965687}. Note=An
CC amphitropic protein able to integrate into the inner leaflet of the
CC outer membrane, probably via amphipathic helices 7 and 8
CC (PubMed:21965687). It has no surface-exposed domains (PubMed:16159783).
CC {ECO:0000269|PubMed:16159783, ECO:0000305|PubMed:21965687}.
CC -!- DOMAIN: Forms a U-shaped beta-half-barrel with a large hydrophobic
CC cavity (3549 Angstroms(3)). The cavity is opened when amphipathic
CC helices 2, 3 and 9 move away from helices 7 and 8 (PubMed:21965687).
CC Has 5 potential amphipathic helices (P1 to P5, residues 56 to 63, 155
CC to 162, 194 to 202, 240 to 250, and 270 to 279 respectively); P2, P3
CC and P5 form helices in the presence of lipid vesicles
CC (PubMed:16159783). {ECO:0000269|PubMed:16159783,
CC ECO:0000269|PubMed:21965687}.
CC -!- PTM: Palmitoylated upon expression of a fusion protein with first 46
CC residues fused to PhoA in E.coli. {ECO:0000269|PubMed:16159783}.
CC -!- BIOTECHNOLOGY: Recognized by sera from 43/43 syphilis patients, it
CC shows promise as a diagnostic antigen (PubMed:12904373). In diagnostic
CC tests for syphilis this protein exhibits a sensitivity of 98% and a
CC specificity of 100%. A fusion with TP0453 (residues 32-287 of TP0453
CC fused N-terminally to residues 38-450 of TP0326) exhibits a sensitivity
CC of 98% and a specificity of 99%, and both proteins exhibit superior
CC accuracy in classifying analytical false-positive samples than a
CC commericially available test, making them candiates for diagnosis
CC (PubMed:23100335). {ECO:0000269|PubMed:12904373,
CC ECO:0000269|PubMed:23100335}.
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; AF007220; AAC18996.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65443.1; -; Genomic_DNA.
DR EMBL; CP004010; AGN75647.1; -; Genomic_DNA.
DR PIR; F71322; F71322.
DR RefSeq; WP_010881902.1; NC_021490.2.
DR PDB; 3K8G; X-ray; 1.95 A; A/B=27-287.
DR PDB; 3K8H; X-ray; 2.39 A; A/B=27-287.
DR PDB; 3K8I; X-ray; 2.20 A; A=27-287.
DR PDB; 3K8J; X-ray; 2.20 A; A=27-287.
DR PDBsum; 3K8G; -.
DR PDBsum; 3K8H; -.
DR PDBsum; 3K8I; -.
DR PDBsum; 3K8J; -.
DR AlphaFoldDB; O67998; -.
DR SMR; O67998; -.
DR IntAct; O67998; 4.
DR STRING; 243276.TPANIC_0453; -.
DR TCDB; 1.B.45.1.1; the treponema porin (t-por) family.
DR EnsemblBacteria; AAC65443; AAC65443; TP_0453.
DR EnsemblBacteria; AGN75647; AGN75647; TPANIC_0453.
DR GeneID; 57878976; -.
DR KEGG; tpa:TP_0453; -.
DR KEGG; tpw:TPANIC_0453; -.
DR PATRIC; fig|243276.9.peg.452; -.
DR eggNOG; ENOG50302A1; Bacteria.
DR HOGENOM; CLU_979835_0_0_12; -.
DR OMA; EAMFSER; -.
DR OrthoDB; 1462388at2; -.
DR EvolutionaryTrace; O67998; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Lipoprotein; Membrane; Palmitate;
KW Reference proteome; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT CHAIN 25..287
FT /note="Outer membrane protein TP0453"
FT /id="PRO_0000434873"
FT REGION 36..40
FT /note="Amphipathic helix 1"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 56..63
FT /note="Amphipathic helix 2"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 69..77
FT /note="Amphipathic helix 3"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 103..112
FT /note="Amphipathic helix 4"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 155..162
FT /note="Amphipathic helix 5"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 172..179
FT /note="Amphipathic helix 6"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 194..202
FT /note="Amphipathic helix 7"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 240..250
FT /note="Amphipathic helix 8"
FT /evidence="ECO:0000305|PubMed:21965687"
FT REGION 270..279
FT /note="Amphipathic helix 9"
FT /evidence="ECO:0000305|PubMed:21965687"
FT LIPID 25
FT /note="N-palmitoyl cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT LIPID 25
FT /note="S-diacylglycerol cysteine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT MUTAGEN 62
FT /note="I->E: No change in detergent partitioning, vesicle
FT associated."
FT /evidence="ECO:0000269|PubMed:21965687"
FT MUTAGEN 162
FT /note="L->E: No change in detergent partitioning, vesicle
FT associated."
FT /evidence="ECO:0000269|PubMed:21965687"
FT MUTAGEN 201
FT /note="L->E: Partitions into detergent and aqueous phase,
FT decreased vesicle association."
FT /evidence="ECO:0000269|PubMed:21965687"
FT MUTAGEN 249
FT /note="V->E: No longer partitions into detergent, no
FT vesicle association, decreased dimer formation."
FT /evidence="ECO:0000269|PubMed:21965687"
FT MUTAGEN 277
FT /note="I->E: No change in detergent partitioning, vesicle
FT associated, decreased dimer formation. Amphipathic peptide
FT (residues 270 to 280) no longer forms alpha helices in the
FT presence of lipid vesicles."
FT /evidence="ECO:0000269|PubMed:16159783,
FT ECO:0000269|PubMed:21965687"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3K8I"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 45..52
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 56..66
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 70..77
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 79..87
FT /evidence="ECO:0007829|PDB:3K8G"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 92..99
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 142..149
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 155..160
FT /evidence="ECO:0007829|PDB:3K8G"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 172..178
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 187..192
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 214..221
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 224..232
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 240..250
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:3K8G"
FT STRAND 260..269
FT /evidence="ECO:0007829|PDB:3K8G"
FT HELIX 270..278
FT /evidence="ECO:0007829|PDB:3K8G"
SQ SEQUENCE 287 AA; 32000 MW; 692712D8891CC03F CRC64;
MIRRRYRGCT QGAWIVSVGM LFASCTSGAW KASVDPLGVV GSGADVYLYF PVAGNENLIS
RIIENHESKA DIKKIVDRTT AVYGAFFARS KEFRLFGSGS YPYAFTNLIF SRSDGWASTK
TEHGITYYES EHTDVSIPAP HFSCVIFGSS KRERMSKMLS RLVNPDRPQL PPRFEKECTS
EGTSQTVALY IKNGGHFITK LLNFPQLNLP LGAMELYLTA RRNEYLYTLS LQLGNAKINF
PIQFLISRVL NAHIHVEGDR LIIEDGTISA ERLASVISSL YSKKGSS
