TONB_SALTY
ID TONB_SALTY Reviewed; 242 AA.
AC P25945;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Protein TonB;
GN Name=tonB; OrderedLocusNames=STM1737;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2266561; DOI=10.1016/s0022-2836(99)80009-6;
RA Hannavy K., Barr G.C., Dorman C.J., Adamson J., Mazengera L.R.,
RA Gallagher M.P., Evans J.S., Levine B.A., Trayer I.P., Higgins C.F.;
RT "TonB protein of Salmonella typhimurium. A model for signal transduction
RT between membranes.";
RL J. Mol. Biol. 216:897-910(1990).
RN [2]
RP SEQUENCE REVISION TO 42; 58-60 AND 168.
RX PubMed=8316087; DOI=10.1111/j.1365-2958.1993.tb01581.x;
RA Karlsson M., Hannavy K., Higgins C.F.;
RT "A sequence-specific function for the N-terminal signal-like sequence of
RT the TonB protein.";
RL Mol. Microbiol. 8:379-388(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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 such as cobalamin, and various
CC iron compounds (such as iron dicitrate, enterochelin, aerobactin,
CC etc.). In the absence of TonB these receptors bind their substrates but
CC do not carry out active transport. TonB also interacts with some
CC colicins and is involved in the energy-dependent, irreversible steps of
CC bacteriophages phi 80 and T1 infection. 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.
CC -!- SUBUNIT: Homodimer. Forms a complex with the accessory proteins ExbB
CC and ExbD (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Single-pass membrane
CC protein; Periplasmic side.
CC -!- SIMILARITY: Belongs to the TonB family. {ECO:0000305}.
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DR EMBL; X56434; CAA39818.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20655.1; -; Genomic_DNA.
DR PIR; S13257; S13257.
DR RefSeq; NP_460696.1; NC_003197.2.
DR RefSeq; WP_001520573.1; NC_003197.2.
DR AlphaFoldDB; P25945; -.
DR BMRB; P25945; -.
DR SMR; P25945; -.
DR STRING; 99287.STM1737; -.
DR PaxDb; P25945; -.
DR EnsemblBacteria; AAL20655; AAL20655; STM1737.
DR GeneID; 1253256; -.
DR KEGG; stm:STM1737; -.
DR PATRIC; fig|99287.12.peg.1833; -.
DR HOGENOM; CLU_098618_0_0_6; -.
DR PhylomeDB; P25945; -.
DR BioCyc; SENT99287:STM1737-MON; -.
DR Proteomes; UP000001014; 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:0043213; P:bacteriocin transport; IEA:UniProtKB-KW.
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 3: Inferred from homology;
KW Bacteriocin transport; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Repeat; Signal-anchor;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..242
FT /note="Protein TonB"
FT /id="PRO_0000196209"
FT TRANSMEM 1..32
FT /note="Helical; Signal-anchor"
FT /evidence="ECO:0000250"
FT TOPO_DOM 33..242
FT /note="Periplasmic"
FT /evidence="ECO:0000250"
FT REPEAT 70..71
FT /note="1-1"
FT REPEAT 72..73
FT /note="1-2"
FT REPEAT 74..75
FT /note="1-3"
FT REPEAT 76..77
FT /note="1-4"
FT REPEAT 78..79
FT /note="1-5"
FT REPEAT 80..81
FT /note="1-6; approximate"
FT REPEAT 82..83
FT /note="1-7"
FT REPEAT 93..94
FT /note="2-1"
FT REPEAT 95..96
FT /note="2-2"
FT REPEAT 97..98
FT /note="2-3"
FT REPEAT 99..100
FT /note="2-4"
FT REPEAT 101..102
FT /note="2-5"
FT REPEAT 103..104
FT /note="2-6"
FT REPEAT 105..106
FT /note="2-7"
FT REGION 55..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..83
FT /note="7 X 2 AA approximate tandem repeats of E-P"
FT REGION 93..106
FT /note="7 X 2 AA approximate tandem repeats of K-P"
FT COMPBIAS 105..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 242 AA; 26294 MW; 7648F6BB3150FA6E CRC64;
MTLDLPRRFP WPTLLSVGIH GAVVAGLLYT SVHQVIELPA PAQPITVTMV SPADLEPPQA
VQPPPEPVVE PEPEPEPEPI PEPPKEAPVV IEKPKPKPKP KPKPKPVKKV EEQPKREVKP
AAPRPASPFE NSAPVRPTSS TASATSKPAV SVPTGPRALS RNQPQYPARA QALRIEGRVK
VKFDVTSAGR VENVQILSAQ PANMFEREVK NAMRKWRYEA GKPGSGLVVN IIFRLNGTAQ
IE
