ID Q138A0_RHOPS Unreviewed; 265 AA.
AC Q138A0;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=Biopolymer transport protein ExbB {ECO:0000256|ARBA:ARBA00022093};
DE Flags: Precursor;
GN OrderedLocusNames=RPD_2357 {ECO:0000313|EMBL:ABE39589.1};
OS Rhodopseudomonas palustris (strain BisB5).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE39589.1, ECO:0000313|Proteomes:UP000001818};
RN [1] {ECO:0000313|EMBL:ABE39589.1, ECO:0000313|Proteomes:UP000001818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB5 {ECO:0000313|EMBL:ABE39589.1,
RC ECO:0000313|Proteomes:UP000001818};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL Submitted (MAR-2006) 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}.
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DR EMBL; CP000283; ABE39589.1; -; Genomic_DNA.
DR AlphaFoldDB; Q138A0; -.
DR STRING; 316057.RPD_2357; -.
DR KEGG; rpd:RPD_2357; -.
DR eggNOG; COG0811; Bacteria.
DR HOGENOM; CLU_053325_0_2_5; -.
DR Proteomes; UP000001818; Chromosome.
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}; Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..265
FT /note="Biopolymer transport protein ExbB"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004181781"
FT TRANSMEM 56..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 163..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..229
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 133..234
FT /note="MotA/TolQ/ExbB proton channel"
FT /evidence="ECO:0000259|Pfam:PF01618"
SQ SEQUENCE 265 AA; 27511 MW; 34C061647D32B709 CRC64;
MTRPRQNGGT RGALAAAWLA AASLLSANAG IAASADMAAL PRDLSPWGMF VNADMVVRTV
MIGLALASLA AWTVWLAKSI ELRRNVTLAR RGLDLLDNGA TLAQVEAECG EDSDTVAQMI
RSVAREASLS GGIQDDGFAD RVSLRLERVE AAAVRRVAIG TGLLASIGAV APFVGLFGTV
WGIMNAFIGI SKANTTNLAV VAPGIAEALL ATALGLVAAI PAVVIYNHLS RRIGSYRALL
GDASAQLLLL IGREAARQRC GRRAA
//
