ID   TONB_XANCB              Reviewed;         223 AA.
AC   B0RLE5; O34261;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Protein TonB;
GN   Name=tonB; OrderedLocusNames=xcc-b100_0008;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9371459; DOI=10.1128/jb.179.22.7103-7110.1997;
RA   Wiggerich H.G., Klauke B., Koeplin R., Priefer U.B., Puehler A.;
RT   "Unusual structure of the tonB-exb DNA region of Xanthomonas campestris pv.
RT   campestris: tonB, exbB, and exbD1 are essential for ferric iron uptake, but
RT   exbD2 is not.";
RL   J. Bacteriol. 179:7103-7110(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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   -!- SUBUNIT: Homodimer. Forms a complex with the accessory proteins ExbB
CC       and ExbD (By 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; Z95386; CAB08610.1; -; Genomic_DNA.
DR   EMBL; AM920689; CAP49336.1; -; Genomic_DNA.
DR   RefSeq; WP_011035266.1; NC_003902.1.
DR   AlphaFoldDB; B0RLE5; -.
DR   SMR; B0RLE5; -.
DR   KEGG; xca:xcc-b100_0008; -.
DR   HOGENOM; CLU_076057_5_0_6; -.
DR   OMA; DCYLHLK; -.
DR   Proteomes; UP000001188; Chromosome.
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; Repeat;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..223
FT                   /note="Protein TonB"
FT                   /id="PRO_0000339185"
FT   TOPO_DOM        1..23
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        24..44
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        45..223
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          61..143
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        63..130
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   223 AA;  23598 MW;  D7C6886FDF06FDA9 CRC64;
     MTEQLVIHRH DYDAGNQGLS WARIIGIAFV IALHLTALMM LLIPAVAPKA PAEKERTTMV
     TLVDAPPPPP PPPPPPPPED KPPPPVKNLS PPKPSPVPPP PEAPVVDVPE PRPSDIVTPP
     SPPAPPAPPS DIGASVDISS KNMNPPKYPP AAFRAGVQGE VILIVDVDAN GNVTNVSVEK
     SSRNRDLDRA AMDAARKWKF NASTVNGQKA AGRVRVPVNF ALN