ID   A0A1G8CPA2_9BURK        Unreviewed;       238 AA.
AC   A0A1G8CPA2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN   ORFNames=SAMN05444748_101436 {ECO:0000313|EMBL:SDH46690.1};
OS   Variovorax sp. OV700.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882826 {ECO:0000313|EMBL:SDH46690.1, ECO:0000313|Proteomes:UP000199505};
RN   [1] {ECO:0000313|Proteomes:UP000199505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV700 {ECO:0000313|Proteomes:UP000199505};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) 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; FNDR01000001; SDH46690.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8CPA2; -.
DR   STRING; 1882826.SAMN05444748_101436; -.
DR   OrthoDB; 9805133at2; -.
DR   Proteomes; UP000199505; 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   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   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        127..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        174..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          100..202
FT                   /note="MotA/TolQ/ExbB proton channel"
FT                   /evidence="ECO:0000259|Pfam:PF01618"
SQ   SEQUENCE   238 AA;  25516 MW;  0DC002C63A7BC686 CRC64;
     MDSQFGLMNV WNQGDFVTKA VAVLLIGMSL VSWIVIIIKA LDVIKYKRLA KHSQDFWHSE
     DFATALNKLG KDDGNPFRAL ALEGREAAAH HRNTKAHLHD ALDVSDWITR ALRNGIDAFT
     ARLQTGLAIL ASVGSTAPFI GLFGTVWGIY HALMSISTAG QATIDKVAGP IGEALIMTAL
     GLAVAIPAVL GYNALVRGNK FVLTKLNSFA HDLHAYFVTG ARVQSGTGDA IVVPLKKG
//