TONB_NEIGO
ID TONB_NEIGO Reviewed; 283 AA.
AC O06432;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Protein TonB;
GN Name=tonB;
OS Neisseria gonorrhoeae.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=485;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FA19;
RX PubMed=9140974; DOI=10.1046/j.1365-2958.1997.3421692.x;
RA Biswas G.D., Anderson J.E., Sparling P.F.;
RT "Cloning and functional characterization of Neisseria gonorrhoeae tonB,
RT exbB and exbD genes.";
RL Mol. Microbiol. 24:169-179(1997).
CC -!- FUNCTION: Pathways of utilization of iron bound to transferrin,
CC lactoferrin and hemoglobin but not to haemin or citrate where dependent
CC on the TonB system.
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; U79563; AAC45286.1; -; Genomic_DNA.
DR RefSeq; WP_003693736.1; NZ_WHPL01000002.1.
DR AlphaFoldDB; O06432; -.
DR SMR; O06432; -.
DR PRIDE; O06432; -.
DR GeneID; 66753585; -.
DR OMA; SEAQAYN; -.
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.
FT CHAIN 1..283
FT /note="Protein TonB"
FT /id="PRO_0000196201"
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..283
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT REGION 52..216
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..136
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 283 AA; 28749 MW; 3CD3F8353B445748 CRC64;
MDKERILTPA VVFSVALLHL AIVALLWQAH KLPVIESGNV IEFVDLGDFG GGGGAPEGAG
APAAPEPQPA PDPPKPVEPP KPVLKPAVTK KADADIQQPK EKPKPEEKPK PEPEPEAKPA
PKPAEKPAEK PSEKPAEHSG NASAKAGSEQ GNGEGKGTGT KGDGTGRGEG SGKGSGGAKG
EHGEGAGGSG GGTGVGSSKG NPLRANGSIP RPAYPALSME NDEQGMVVLS VLVSPGGHVE
SVKVVKSSGF SRLDNAARKA AQNGHFQANA WTEFKVPVKF ELN