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Database: UniProt/TrEMBL
Entry: B8GL23_THISH
LinkDB: B8GL23_THISH
Original site: B8GL23_THISH 
ID   B8GL23_THISH            Unreviewed;       284 AA.
AC   B8GL23;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Protein TonB {ECO:0000256|ARBA:ARBA00022362, ECO:0000256|RuleBase:RU362123};
DE   Flags: Precursor;
GN   OrderedLocusNames=Tgr7_0443 {ECO:0000313|EMBL:ACL71541.1};
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588 {ECO:0000313|EMBL:ACL71541.1, ECO:0000313|Proteomes:UP000002383};
RN   [1] {ECO:0000313|EMBL:ACL71541.1, ECO:0000313|Proteomes:UP000002383}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7 {ECO:0000313|EMBL:ACL71541.1,
RC   ECO:0000313|Proteomes:UP000002383};
RX   PubMed=21475584;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL71541.1; -; Genomic_DNA.
DR   RefSeq; WP_012637030.1; NC_011901.1.
DR   AlphaFoldDB; B8GL23; -.
DR   STRING; 396588.Tgr7_0443; -.
DR   KEGG; tgr:Tgr7_0443; -.
DR   eggNOG; COG0810; Bacteria.
DR   HOGENOM; CLU_979828_0_0_6; -.
DR   OMA; SEAQAYN; -.
DR   OrthoDB; 6077935at2; -.
DR   Proteomes; UP000002383; 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|RuleBase:RU362123};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002383};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968,
KW   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   DOMAIN          206..282
FT                   /note="TonB C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03544"
FT   REGION          43..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..132
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..168
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   284 AA;  31558 MW;  716627F9065A62F5 CRC64;
     MRPFLFALLI SVLVHLVLLW GDWAMPVLQR DVSLPGSRPL DVALMPARPT QPEPEPLSSA
     EPEPEPEPEP EPEPEPEPEP EPEPEPEPEP EPEPEPEPEP EPEPEPEPEP EPEPEPEPEP
     EPEPEPEPEP EPAVEQVPEP REDPAPATPR ESVPVERSEP DAERQRPEAV MPPAEPVTPQ
     DAPSETLDAD LMADYQDRLR AAIEREKRYP RLAVRQQLQG IALVGFRVLG DGRIEAIRLM
     ESSGHNLLDE AALAAVRQVG RAQPLPAGAG PFRDFEIALE FKLF
//
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