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TONB_CAMCO
ID   TONB_CAMCO              Reviewed;         232 AA.
AC   O07650;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Protein TonB;
GN   Name=tonB;
OS   Campylobacter coli.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Campylobacteraceae; Campylobacter.
OX   NCBI_TaxID=195;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=VC167;
RX   PubMed=9190817; DOI=10.1128/jb.179.12.3997-4002.1997;
RA   Guerry P., Perez-Casal J., Yao R., McVeigh A., Trust T.J.;
RT   "A genetic locus involved in iron utilization unique to some Campylobacter
RT   strains.";
RL   J. Bacteriol. 179:3997-4002(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; U80812; AAC45420.1; -; Genomic_DNA.
DR   RefSeq; WP_002837894.1; NZ_UIGL01000002.1.
DR   AlphaFoldDB; O07650; -.
DR   SMR; O07650; -.
DR   STRING; 195.ATE51_02140; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   InterPro; IPR006260; TonB/TolA_C.
DR   InterPro; IPR037682; TonB_C.
DR   Pfam; PF03544; TonB_C; 1.
DR   TIGRFAMs; TIGR01352; tonB_Cterm; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..232
FT                   /note="Protein TonB"
FT                   /id="PRO_0000196193"
FT   TOPO_DOM        1..12
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        13..29
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..232
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          59..82
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        59..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   232 AA;  26992 MW;  40CD3E72D2E2561E CRC64;
     MKTFISNHKN QSSFITLFVF TPLFFVFLYS KDFLHIQPNE TIKENKFNMA IKHFVQNSSD
     MKPTQPTQTI QEPSNVQPKE PVQEIKKIKP RKEKLIAKPK KIIPPANAKA ISQPKKDTNM
     QQPIMQQQTP QASSYQSVAL TSNSEFLKEI KSAIDEALIY PRQARKMRMS GEVLVEFTWT
     KEKKLENLKI LKPSKYDFLN KSALETIRIA SKKFPQYEKT FHIKIPLVYK LS
 
 
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