ID I4Z6C6_9BURK Unreviewed; 220 AA.
AC I4Z6C6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN ORFNames=LepocDRAFT_00005090 {ECO:0000313|EMBL:EIM31768.1};
OS Leptothrix ochracea L12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=735332 {ECO:0000313|EMBL:EIM31768.1, ECO:0000313|Proteomes:UP000053899};
RN [1] {ECO:0000313|EMBL:EIM31768.1, ECO:0000313|Proteomes:UP000053899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EIM31768.1,
RC ECO:0000313|Proteomes:UP000053899};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stepanauskas R., Masland D.,
RA Poulton N., Emerson D., Fleming E., Woyke T.;
RT "Improved High-Quality Draft sequence of Leptothrix ochracea L12.";
RL Submitted (APR-2012) 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; JH660667; EIM31768.1; -; Genomic_DNA.
DR RefSeq; WP_009453153.1; NZ_JH660667.1.
DR AlphaFoldDB; I4Z6C6; -.
DR HOGENOM; CLU_053325_2_0_4; -.
DR OrthoDB; 9805133at2; -.
DR Proteomes; UP000053899; 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:UP000053899};
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 13..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 94..199
FT /note="MotA/TolQ/ExbB proton channel"
FT /evidence="ECO:0000259|Pfam:PF01618"
SQ SEQUENCE 220 AA; 23418 MW; 6242538EF6234B75 CRC64;
MGSFWQIWSE GDAIHRVVAS VLLLMSMSAW VLILWKSWIL VRARRDLALA VPAFWAAPDW
AAARLQMDAL DREQVALPLL DAALQTPPAG TLEAAGDVGA QLTRRLRDAL HGVLTQLQFG
QVLLASIGAT APFIGLFGTV WGIYHALLGI SASGSMGIDK VAGPVGEALI MTAAGLAVAI
PAVLAYNVFG KWVGACEAEL EGFAHDLREM VLQDHGLRSA
//
