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Database: UniProt
Entry: A0A109BDK3_HYPSL
LinkDB: A0A109BDK3_HYPSL
Original site: A0A109BDK3_HYPSL 
ID   A0A109BDK3_HYPSL        Unreviewed;       319 AA.
AC   A0A109BDK3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN   ORFNames=APY04_2235 {ECO:0000313|EMBL:KWT66828.1};
OS   Hyphomicrobium sulfonivorans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=121290 {ECO:0000313|EMBL:KWT66828.1, ECO:0000313|Proteomes:UP000059074};
RN   [1] {ECO:0000313|EMBL:KWT66828.1, ECO:0000313|Proteomes:UP000059074}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDL6 {ECO:0000313|EMBL:KWT66828.1,
RC   ECO:0000313|Proteomes:UP000059074};
RA   Albers P.;
RT   "Transcriptomic analysis of a linuron degrading triple-species bacterial
RT   consortium.";
RL   Submitted (OCT-2015) 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   -!- 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KWT66828.1}.
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DR   EMBL; LMTR01000071; KWT66828.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A109BDK3; -.
DR   STRING; 121290.APY04_2235; -.
DR   PATRIC; fig|121290.4.peg.2433; -.
DR   OrthoDB; 9805133at2; -.
DR   Proteomes; UP000059074; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   InterPro; IPR002898; MotA_ExbB_proton_chnl.
DR   InterPro; IPR014164; TonB_ExbB_1.
DR   NCBIfam; TIGR02797; exbB; 1.
DR   PANTHER; PTHR30625:SF16; BIOPOLYMER TRANSPORT PROTEIN EXBB; 1.
DR   PANTHER; PTHR30625; PROTEIN TOLQ; 1.
DR   Pfam; PF01618; MotA_ExbB; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
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:UP000059074};
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        106..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..236
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        256..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          169..286
FT                   /note="MotA/TolQ/ExbB proton channel"
FT                   /evidence="ECO:0000259|Pfam:PF01618"
FT   REGION          1..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        27..41
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   319 AA;  33027 MW;  319D64A7B99C02A7 CRC64;
     MPAAPTTTPS TAGAQFAPAS DAAPQMGGFQ PGSQANDLSQ GLTAPPAAAA DAAPVDQPHE
     ISNSLGTGLV DGATDEPALA ASESVGSELH VPHDLSPWGM FMAADIVVKT VMVGLVLASV
     ATWTIWLAKS IELMAARSRM RRALRKLAAA NSMSEAMSLI DAKRGPVPAM LRAAIAETRA
     SWDLPDKYAI KDRIKARLER IELASGRDVA RGTGMLATVG STAPFIGLFG TVWGIMNSFI
     GIAETQTTNL AVVAPGIAEA LLATAFGLIA AIPAVMIYNH FARSIAGYKA LVGDASVAVL
     GIVSRDFDRG VRPELRAAE
//
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