ID A0A258YYR0_9PROT Unreviewed; 256 AA.
AC A0A258YYR0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
GN ORFNames=B7Y21_06240 {ECO:0000313|EMBL:OYZ57804.1};
OS Hydrogenophilales bacterium 16-61-112.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970519 {ECO:0000313|EMBL:OYZ57804.1, ECO:0000313|Proteomes:UP000216368};
RN [1] {ECO:0000313|EMBL:OYZ57804.1, ECO:0000313|Proteomes:UP000216368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-61-112 {ECO:0000313|EMBL:OYZ57804.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-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}.
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:OYZ57804.1}.
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DR EMBL; NCHD01000024; OYZ57804.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258YYR0; -.
DR Proteomes; UP000216368; 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 22..42
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 182..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 102..213
FT /note="MotA/TolQ/ExbB proton channel"
FT /evidence="ECO:0000259|Pfam:PF01618"
SQ SEQUENCE 256 AA; 27695 MW; E2F69164F2F5005E CRC64;
METAATQTQL GFAHFIAQAD GLAHFLLVVL LAMSVITWYL IVSKSVTNWH MKKHAQAFLA
RFWDAPGLAS VANYLQNHGV NDPFSHLTHH GLKAAEQYRN KTGQRLIESG SEDEFLTRAL
RRAINQDTAR LEYGHTMLAS IASSAPFVGL FGTVWGIYHA LVNIGMSGSG SLDQVAGPVG
EALIMTALGL AVAIPAVLAY NFFNRAKRQM LSEVDGFAHD LFAFMSTGVR NNTRIEKDAA
QVYTASAQTA PVAGSA
//
