TPF1_TREPA
ID TPF1_TREPA Reviewed; 177 AA.
AC P16665;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 137.
DE RecName: Full=Antigen TpF1;
DE AltName: Full=Antigen 4D;
DE AltName: Full=Antigen C1-5;
GN Name=tpf1; OrderedLocusNames=TP_1038;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-12.
RC STRAIN=Nichols;
RX PubMed=2471912; DOI=10.1016/0882-4010(89)90005-3;
RA Noordhoek G.T., Hermans P.W.M., Paul A.N., Schouls L.M.,
RA van der Sluis J.J., van Embden J.D.A.;
RT "Treponema pallidum subspecies pallidum (Nichols) and Treponema pallidum
RT subspecies pertenue (CDC 2575) differ in at least one nucleotide:
RT comparison of two homologous antigens.";
RL Microb. Pathog. 6:29-42(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2643579; DOI=10.1128/iai.57.2.633-635.1989;
RA Walfield A.M., Roche E.S., Zounes M.C., Kirkpatrick H., Wild M.A.,
RA Textor G., Tsai P.K., Richardson C.;
RT "Primary structure of an oligomeric antigen of Treponema pallidum.";
RL Infect. Immun. 57:633-635(1989).
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).
RN [4]
RP DISULFIDE BONDS.
RC STRAIN=Nichols;
RX PubMed=3549683; DOI=10.1128/jb.169.4.1365-1371.1987;
RA Radolf J.D., Borenstein L.A., Kim J.Y., Fehniger T.E., Lovett M.A.;
RT "Role of disulfide bonds in the oligomeric structure and protease
RT resistance of recombinant and native Treponema pallidum surface antigen
RT 4D.";
RL J. Bacteriol. 169:1365-1371(1987).
CC -!- FUNCTION: May play an important structural role in the outer membrane.
CC -!- SUBUNIT: Homodecamer; either linked or stabilized by disulfide bonds.
CC -!- SIMILARITY: Belongs to the Dps family. {ECO:0000305}.
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DR EMBL; M32401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AE000520; AAC26592.1; -; Genomic_DNA.
DR PIR; JS0097; JS0097.
DR RefSeq; WP_010882482.1; NC_021490.2.
DR PDB; 2FJC; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=22-177.
DR PDBsum; 2FJC; -.
DR AlphaFoldDB; P16665; -.
DR SMR; P16665; -.
DR IntAct; P16665; 3.
DR STRING; 243276.TPANIC_1038; -.
DR EnsemblBacteria; AAC26592; AAC26592; TP_1038.
DR KEGG; tpa:TP_1038; -.
DR eggNOG; COG0783; Bacteria.
DR HOGENOM; CLU_098183_2_2_12; -.
DR OMA; KKYHWDV; -.
DR OrthoDB; 1742631at2; -.
DR EvolutionaryTrace; P16665; -.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0008199; F:ferric iron binding; IEA:InterPro.
DR GO; GO:0016722; F:oxidoreductase activity, acting on metal ions; IEA:InterPro.
DR CDD; cd01043; DPS; 1.
DR Gene3D; 1.20.1260.10; -; 1.
DR InterPro; IPR002177; DPS_DNA-bd.
DR InterPro; IPR023188; DPS_DNA-bd_CS.
DR InterPro; IPR012347; Ferritin-like.
DR InterPro; IPR009078; Ferritin-like_SF.
DR InterPro; IPR008331; Ferritin_DPS_dom.
DR PANTHER; PTHR42932; PTHR42932; 1.
DR Pfam; PF00210; Ferritin; 1.
DR PIRSF; PIRSF005900; Dps; 1.
DR PRINTS; PR01346; HELNAPAPROT.
DR SUPFAM; SSF47240; SSF47240; 1.
DR PROSITE; PS00818; DPS_1; 1.
DR PROSITE; PS00819; DPS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2471912"
FT CHAIN 2..177
FT /note="Antigen TpF1"
FT /id="PRO_0000201664"
FT HELIX 29..59
FT /evidence="ECO:0007829|PDB:2FJC"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:2FJC"
FT HELIX 65..92
FT /evidence="ECO:0007829|PDB:2FJC"
FT HELIX 101..107
FT /evidence="ECO:0007829|PDB:2FJC"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:2FJC"
FT HELIX 120..147
FT /evidence="ECO:0007829|PDB:2FJC"
FT HELIX 151..175
FT /evidence="ECO:0007829|PDB:2FJC"
SQ SEQUENCE 177 AA; 19361 MW; A0E0855069566773 CRC64;
MNMCTDGKKY HSTATSAAVG ASAPGVPDAR AIAAICEQLR QHVADLGVLY IKLHNYHWHI
YGIEFKQVHE LLEEYYVSVT EAFDTIAERL LQLGAQAPAS MAEYLALSGI AEETEKEITI
VSALARVKRD FEYLSTRFSQ TQVLAAESGD AVTDGIITDI LRTLGKAIWM LGATLKA
