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TONB_HELPY
ID   TONB_HELPY              Reviewed;         285 AA.
AC   O25899;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 113.
DE   RecName: Full=Protein TonB;
GN   Name=tonB; OrderedLocusNames=HP_1341;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA   Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA   Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA   McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA   Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA   Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA   Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Interacts with outer membrane receptor proteins that carry
CC       out high-affinity binding and energy dependent uptake into the
CC       periplasmic space of specific substrates. It could act to transduce
CC       energy from the cytoplasmic membrane to specific energy-requiring
CC       processes in the outer membrane, resulting in the release into the
CC       periplasm of ligands bound by these outer membrane proteins (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the TonB family. {ECO:0000305}.
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DR   EMBL; AE000511; AAD08383.1; -; Genomic_DNA.
DR   PIR; E64687; E64687.
DR   RefSeq; NP_208133.1; NC_000915.1.
DR   RefSeq; WP_000703807.1; NC_018939.1.
DR   PDB; 5LW8; NMR; -; A=194-285.
DR   PDB; 6SLY; NMR; -; A=179-285.
DR   PDBsum; 5LW8; -.
DR   PDBsum; 6SLY; -.
DR   AlphaFoldDB; O25899; -.
DR   BMRB; O25899; -.
DR   SMR; O25899; -.
DR   IntAct; O25899; 1.
DR   MINT; O25899; -.
DR   STRING; 85962.C694_06920; -.
DR   PaxDb; O25899; -.
DR   EnsemblBacteria; AAD08383; AAD08383; HP_1341.
DR   KEGG; hpy:HP_1341; -.
DR   PATRIC; fig|85962.47.peg.1436; -.
DR   eggNOG; COG0810; Bacteria.
DR   OMA; SEAQAYN; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0098797; C:plasma membrane protein complex; IBA:GO_Central.
DR   GO; GO:0031992; F:energy transducer activity; IBA:GO_Central.
DR   GO; GO:0015343; F:siderophore transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR003538; TonB.
DR   InterPro; IPR006260; TonB/TolA_C.
DR   InterPro; IPR037682; TonB_C.
DR   Pfam; PF03544; TonB_C; 1.
DR   PRINTS; PR01374; TONBPROTEIN.
DR   TIGRFAMs; TIGR01352; tonB_Cterm; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW   Protein transport; Reference proteome; Repeat; Signal-anchor;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..285
FT                   /note="Protein TonB"
FT                   /id="PRO_0000196198"
FT   TOPO_DOM        1..14
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        15..35
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..285
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          55..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..97
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   HELIX           185..189
FT                   /evidence="ECO:0007829|PDB:6SLY"
FT   HELIX           197..208
FT                   /evidence="ECO:0007829|PDB:5LW8"
FT   HELIX           215..218
FT                   /evidence="ECO:0007829|PDB:5LW8"
FT   STRAND          222..230
FT                   /evidence="ECO:0007829|PDB:5LW8"
FT   TURN            232..234
FT                   /evidence="ECO:0007829|PDB:6SLY"
FT   STRAND          236..246
FT                   /evidence="ECO:0007829|PDB:5LW8"
FT   HELIX           248..260
FT                   /evidence="ECO:0007829|PDB:5LW8"
FT   HELIX           262..264
FT                   /evidence="ECO:0007829|PDB:5LW8"
FT   STRAND          274..280
FT                   /evidence="ECO:0007829|PDB:5LW8"
SQ   SEQUENCE   285 AA;  31585 MW;  3897A8BB7B70BDF8 CRC64;
     MKISPSPRKL SKVSTSVSFL ISFALYAIGF GYFLLREDAP EPLAQAGTTK VTMSLASINT
     NSNTKTNAES AKPKEEPKEK PKKEEPKKEE PKKEVTKPKP KPKPKPKPKP KPKPEPKPEP
     KPEPKPEPKV EEVKKEEPKE EPKKEEAKEE AKEKSAPKQV TTKDIVKEKD KQEESNKTSE
     GATSEAQAYN PGVSNEFLMK IQTAISSKNR YPKMAQIRGI EGEVLVSFTI NADGSVTDIK
     VVKSNTTDIL NHAALEAIKS AAHLFPKPEE TVHLKIPIAY SLKED
 
 
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