ID   TONB_SERMA              Reviewed;         247 AA.
AC   P26185;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Protein TonB;
GN   Name=tonB;
OS   Serratia marcescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=W225;
RX   PubMed=1838128; DOI=10.1111/j.1365-2958.1991.tb01986.x;
RA   Gaisser S., Braun V.;
RT   "The tonB gene of Serratia marcescens: sequence, activity and partial
RT   complementation of Escherichia coli tonB mutants.";
RL   Mol. Microbiol. 5:2777-2787(1991).
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 (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; Single-pass membrane
CC       protein; Periplasmic side.
CC   -!- SIMILARITY: Belongs to the TonB family. {ECO:0000305}.
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DR   EMBL; X60996; CAA43308.1; -; Genomic_DNA.
DR   PIR; S18592; S18592.
DR   RefSeq; WP_016927510.1; NZ_WUWF01000012.1.
DR   AlphaFoldDB; P26185; -.
DR   SMR; P26185; -.
DR   STRING; 273526.SMDB11_1948; -.
DR   PRIDE; P26185; -.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0031992; F:energy transducer activity; IEA:InterPro.
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; Repeat; Signal-anchor; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..247
FT                   /note="Protein TonB"
FT                   /id="PRO_0000196210"
FT   TOPO_DOM        1..11
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..35
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        36..247
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REPEAT          76..77
FT                   /note="1-1"
FT   REPEAT          78..79
FT                   /note="1-2"
FT   REPEAT          80..81
FT                   /note="1-3"
FT   REPEAT          82..83
FT                   /note="1-4"
FT   REPEAT          84..85
FT                   /note="1-5"
FT   REPEAT          101..102
FT                   /note="2-1"
FT   REPEAT          103..104
FT                   /note="2-2"
FT   REPEAT          105..106
FT                   /note="2-3"
FT   REPEAT          107..108
FT                   /note="2-4"
FT   REPEAT          109..110
FT                   /note="2-5"
FT   REGION          59..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..85
FT                   /note="5 X 2 AA tandem repeats of E-P"
FT   REGION          101..110
FT                   /note="5 X 2 AA tandem repeats of K-P"
FT   COMPBIAS        60..74
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..128
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   247 AA;  27389 MW;  46EE6E869ED8B64B CRC64;
     MPLKKMFLNR RISVPFVLSV GLHSALVAGL LYASVKEVVE LPKPEDAPIS VMMVNTAAMA
     EPPPPAPAEP EPPQVEPEPE PEPEPIVEPP PKAIVKPEPV KPKPKPKPKP KVEKQVKPEP
     KKVEPREPSP FNNDSPAKPI DKAPVKQAPA APVQGNSREV GPRPISRANP LYPPRAQALQ
     IEGNVRVQFD IDSDGRVSNV RILSAEPRNM FEREVKQAMR KWRYEAKEAK DRTVTIRFKL
     NGTTELN