ID A0A0C5VK97_9GAMM Unreviewed; 289 AA.
AC A0A0C5VK97;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Protein TonB {ECO:0000256|ARBA:ARBA00022362, ECO:0000256|RuleBase:RU362123};
GN ORFNames=YC6258_01744 {ECO:0000313|EMBL:AJQ93788.1};
OS Gynuella sunshinyii YC6258.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Saccharospirillaceae; Gynuella.
OX NCBI_TaxID=1445510 {ECO:0000313|EMBL:AJQ93788.1, ECO:0000313|Proteomes:UP000032266};
RN [1] {ECO:0000313|EMBL:AJQ93788.1, ECO:0000313|Proteomes:UP000032266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YC6258 {ECO:0000313|EMBL:AJQ93788.1,
RC ECO:0000313|Proteomes:UP000032266};
RA Khan H., Chung E.J., Chung Y.R.;
RT "Full genme sequencing of cellulolytic bacterium Gynuella sunshinyii
RT YC6258T gen. nov., sp. nov.";
RL Submitted (JAN-2014) to the EMBL/GenBank/DDBJ databases.
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.
CC {ECO:0000256|RuleBase:RU362123}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004383, ECO:0000256|RuleBase:RU362123}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004383,
CC ECO:0000256|RuleBase:RU362123}; Periplasmic side
CC {ECO:0000256|ARBA:ARBA00004383, ECO:0000256|RuleBase:RU362123}.
CC -!- SIMILARITY: Belongs to the TonB family. {ECO:0000256|ARBA:ARBA00006555,
CC ECO:0000256|RuleBase:RU362123}.
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DR EMBL; CP007142; AJQ93788.1; -; Genomic_DNA.
DR RefSeq; WP_052830142.1; NZ_CP007142.1.
DR AlphaFoldDB; A0A0C5VK97; -.
DR STRING; 1445510.YC6258_01744; -.
DR KEGG; gsn:YC6258_01744; -.
DR PATRIC; fig|1445510.3.peg.1708; -.
DR HOGENOM; CLU_076333_3_0_6; -.
DR Proteomes; UP000032266; Chromosome.
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:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0015891; P:siderophore transport; IEA:InterPro.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR Gene3D; 3.30.1150.10; -; 1.
DR InterPro; IPR003538; TonB.
DR InterPro; IPR006260; TonB/TolA_C.
DR InterPro; IPR037682; TonB_C.
DR NCBIfam; TIGR01352; tonB_Cterm; 1.
DR PANTHER; PTHR33446:SF2; PROTEIN TONB; 1.
DR PANTHER; PTHR33446; PROTEIN TONB-RELATED; 1.
DR Pfam; PF03544; TonB_C; 1.
DR PRINTS; PR01374; TONBPROTEIN.
DR SUPFAM; SSF74653; TolA/TonB C-terminal domain; 1.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519,
KW ECO:0000256|RuleBase:RU362123};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU362123}; Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU362123};
KW Reference proteome {ECO:0000313|Proteomes:UP000032266};
KW Signal {ECO:0000256|SAM:SignalP};
KW Signal-anchor {ECO:0000256|RuleBase:RU362123};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362123}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..289
FT /note="Protein TonB"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002183444"
FT DOMAIN 212..288
FT /note="TonB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03544"
FT REGION 56..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..124
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 289 AA; 31236 MW; 2D69DFFE07D6083B CRC64;
MQNSKVTIAL LASLSLHTAA AAWFFRTTEE TIEMSPAAGS NSQIMTLSMA DFATPVETPP
QADVMPAPTT PDTAAVTEPE PDITPEPEPQ PEPDITPEPE PQPEPDITPE PEPQPEPDIT
PEPEPQPEPE IKPEPKPTPT AKQPSMAKPV TELSASPQPT TTSTTATTQV ASLSSNTPGA
VTSDARAGDN TDTDESARYM AIINALIQRS HRYPDEARQR GQQGQVKLTI TVKPNGKIKK
IKIDKSSGYA LLDREALAIA RRINPLPDFP PSMKQEILEL TFPIEFVLN
//
