ID A0A0A1VF41_9BURK Unreviewed; 238 AA.
AC A0A0A1VF41;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN ORFNames=AVS7_01928 {ECO:0000313|EMBL:GAD22168.1};
OS Acidovorax sp. MR-S7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1268622 {ECO:0000313|EMBL:GAD22168.1};
RN [1] {ECO:0000313|EMBL:GAD22168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-S7 {ECO:0000313|EMBL:GAD22168.1};
RX DOI=10.1128/genomeA.00412-13;
RA Miura T., Kusada H., Kamagata Y., Hanada S., Kimura N.;
RT "Genome Sequence of the Multiple-beta-Lactam-Antibiotic-Resistant Bacterium
RT Acidovorax sp. Strain MR-S7.";
RL Genome Announc. 1:e00412-13(2013).
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; DF238913; GAD22168.1; -; Genomic_DNA.
DR RefSeq; WP_020228201.1; NZ_DF238913.1.
DR AlphaFoldDB; A0A0A1VF41; -.
DR STRING; 1268622.AVS7_01928; -.
DR eggNOG; COG0811; Bacteria.
DR OrthoDB; 9805133at2; -.
DR Proteomes; UP000030646; 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:UP000030646};
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..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..206
FT /note="MotA/TolQ/ExbB proton channel"
FT /evidence="ECO:0000259|Pfam:PF01618"
SQ SEQUENCE 238 AA; 25623 MW; 5D55A946A028C57E CRC64;
MESHFGITNV WIQGDFVTRA VAVLLLGMSL ASWIVIIIKA LDIVKFKKDA RAARDFWHSE
DFAAGLTKLG RDPANPFRHL ALEGREATAH HRNTQAHLHD SLDVSDWVTR CLRNCIDEFT
ARLQSGLAIL ASVGSTAPFI GLFGTVWGIY HALVAIGSSG QSTIDKVAGP IGEALIMTAL
GLAVAIPAVL GYNALVRGNK SILNNLNSFA HDLHAYFVTG ARVNVSSESS KVLPIKKG
//
