ID   TONB_NEIMA              Reviewed;         280 AA.
AC   P57003; A1ITH9;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Protein TonB;
GN   Name=tonB; OrderedLocusNames=NMA1985;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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. Required
CC       for heme utilization and virulence.
CC   -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a complex
CC       with TonB. {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; AL157959; CAM09094.1; -; Genomic_DNA.
DR   PIR; F81827; F81827.
DR   RefSeq; WP_002236738.1; NC_003116.1.
DR   AlphaFoldDB; P57003; -.
DR   SMR; P57003; -.
DR   EnsemblBacteria; CAM09094; CAM09094; NMA1985.
DR   KEGG; nma:NMA1985; -.
DR   HOGENOM; CLU_899630_0_0_4; -.
DR   OMA; DCYLHLK; -.
DR   BioCyc; NMEN122587:NMA_RS10060-MON; -.
DR   Proteomes; UP000000626; 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: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: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   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Signal-anchor; Transmembrane; Transmembrane helix; Transport; Virulence.
FT   CHAIN           1..280
FT                   /note="Protein TonB"
FT                   /id="PRO_0000196202"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..27
FT                   /note="Helical; Signal-anchor"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        28..280
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          51..217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..83
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..142
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   280 AA;  29211 MW;  3282EA3B9917B1F7 CRC64;
     MDKERILTPA VVFSVALLHL AMVALLWQAH KLPVIESGNV IEFVDLGDFG GGDGAPEGAG
     APAAPEPQPV PEPPKPVEPP KPVLKPVVTK KADADIQQPK EEPKPEEKPK PEEKPKPEPK
     PEAKPVPKPA EKPVEKPSEK PAEHPGNASA KADSEQGNGE DKGTGIKGDG TGRGEGSGKG
     SGGVKGEHGE GAGSSKGNPL RANGSIPRPA YPTLSMENDE QGTVVLSVLV SPGGHVESVK
     IVKSSGFSRL DNAARKAAQN GHFQANAWTE FKVPVKFELN