ID A0A1C3K1N9_9BURK Unreviewed; 301 AA.
AC A0A1C3K1N9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN ORFNames=ODI_01853 {ECO:0000313|EMBL:SBT25429.1}, ODI_R1740
GN {ECO:0000313|EMBL:SOE48937.1};
OS Orrella dioscoreae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Orrella.
OX NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT25429.1, ECO:0000313|Proteomes:UP000078558};
RN [1] {ECO:0000313|EMBL:SBT25429.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT25429.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SOE48937.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE48937.1};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in the TonB-dependent energy-dependent transport of
CC various receptor-bound substrates. Protects ExbD from proteolytic
CC degradation and functionally stabilizes TonB.
CC {ECO:0000256|ARBA:ARBA00024816}.
CC -!- SUBUNIT: The accessory proteins ExbB and ExbD seem to form a complex
CC with TonB. {ECO:0000256|ARBA:ARBA00011471}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004057}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC ECO:0000256|RuleBase:RU004057}.
CC -!- SIMILARITY: Belongs to the exbB/tolQ family.
CC {ECO:0000256|RuleBase:RU004057}.
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DR EMBL; FLRC01000018; SBT25429.1; -; Genomic_DNA.
DR EMBL; LT907988; SOE48937.1; -; Genomic_DNA.
DR RefSeq; WP_067753352.1; NZ_LT907988.1.
DR AlphaFoldDB; A0A1C3K1N9; -.
DR STRING; 1851544.ODI_01853; -.
DR KEGG; odi:ODI_R1740; -.
DR OrthoDB; 9805133at2; -.
DR Proteomes; UP000078558; Chromosome i.
DR Proteomes; UP000078558; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR PANTHER; PTHR30625:SF14; BIOPOLYMER TRANSPORT PROTEIN EXBB; 1.
DR PANTHER; PTHR30625; PROTEIN TOLQ; 1.
DR Pfam; PF01618; MotA_ExbB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW ECO:0000256|RuleBase:RU004057};
KW Reference proteome {ECO:0000313|Proteomes:UP000078558};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU004057}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..301
FT /note="Biopolymer transport protein ExbB"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015062541"
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 157..263
FT /note="MotA/TolQ/ExbB proton channel"
FT /evidence="ECO:0000259|Pfam:PF01618"
SQ SEQUENCE 301 AA; 31820 MW; 8A51B9AF3F6DFD15 CRC64;
MSILMQAAAA MLAQATPSTA EVAPAAAPAA PAAAPAAPLV DSLAPAANAV GGAAADAQMG
FMHFIAQSDM VGKGLFIVLI VMSLVTWYLI VVKAISNMRT RRRSDQFLNT FWNSTSLESV
ENEMRTHGVN DPFSHLTSHA VHARTHHAKY GATRLEEIGS NGEFVTRTMR KVIDEETAKL
ENGLTVLASV GSTAPFVGLF GTVWGVYHAL VGIGMSEGMT INRIAGPVGE ALIMTGLGLA
VAIPAVLAYN TFVRSNRVLL ARLDAFAHDL FAFLSTGQQV VFPDSKVRSL RRSVPGSKGS
E
//