ID A0A0Q6VP01_9BURK Unreviewed; 418 AA.
AC A0A0Q6VP01;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Multidrug transporter {ECO:0000313|EMBL:KQV80292.1};
GN ORFNames=ASD15_15650 {ECO:0000313|EMBL:KQV80292.1};
OS Massilia sp. Root351.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1736522 {ECO:0000313|EMBL:KQV80292.1, ECO:0000313|Proteomes:UP000051876};
RN [1] {ECO:0000313|EMBL:KQV80292.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV80292.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV80292.1, ECO:0000313|Proteomes:UP000051876}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root351 {ECO:0000313|EMBL:KQV80292.1,
RC ECO:0000313|Proteomes:UP000051876};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004519}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004519}. Membrane
CC {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor
CC {ECO:0000256|ARBA:ARBA00004635}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000256|ARBA:ARBA00009477}.
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:KQV80292.1}.
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DR EMBL; LMDJ01000032; KQV80292.1; -; Genomic_DNA.
DR RefSeq; WP_057157593.1; NZ_LMDJ01000032.1.
DR AlphaFoldDB; A0A0Q6VP01; -.
DR OrthoDB; 9783047at2; -.
DR Proteomes; UP000051876; 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:0042221; P:response to chemical; IEA:UniProt.
DR Gene3D; 2.40.30.170; -; 1.
DR Gene3D; 2.40.420.20; -; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR InterPro; IPR043602; CusB_dom_1.
DR InterPro; IPR032317; HlyD_D23.
DR InterPro; IPR006143; RND_pump_MFP.
DR NCBIfam; TIGR01730; RND_mfp; 1.
DR PANTHER; PTHR30158; ACRA/E-RELATED COMPONENT OF DRUG EFFLUX TRANSPORTER; 1.
DR PANTHER; PTHR30158:SF3; MULTIDRUG EFFLUX PUMP SUBUNIT ACRA-RELATED; 1.
DR Pfam; PF00529; CusB_dom_1; 1.
DR Pfam; PF16576; HlyD_D23; 1.
DR SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000051876};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..418
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006294841"
FT DOMAIN 37..360
FT /note="Cation efflux system protein CusB"
FT /evidence="ECO:0000259|Pfam:PF00529"
FT DOMAIN 59..293
FT /note="RND efflux pump membrane fusion protein barrel-
FT sandwich"
FT /evidence="ECO:0000259|Pfam:PF16576"
FT REGION 366..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 418 AA; 42464 MW; 3D847F2A6DC9EAFC CRC64;
MRSVPRCTPV AAAIITLSML AACGKKDDKA GAAPPPPQVA VYTVAPATLT LSTELPGRLE
ASRVAQVRAR TPGIVLQRVY KEGSDVKAGE ILFRIDPAQF QASYDSAQAA VAKAEANLAQ
AELKVKRYKP LLAAQAVSNQ EYDDAVTAQK QAAADLATTR AARTTAGLTL GYATVTSPIS
GRVGRALVTE GALVGQGEAT PMATVQTLDP IYVTITQSST EVLRLQRALA AGKLKGAGNG
AAKVTLVTED GQPYPQSGKL LFSDVAVDET TGSVAMRAEF PNPNRTLLPG MYVRARLEQA
VNEAALQVPQ QAVVRGPEGA TVMVVGADNK VTAVPVKADA AQNGSWIVSS GLKGGERVIV
EGFQKTKPGG TVTPAPWQGP VAATPGGAPA APAPASAPAA AAAPAASAPA AAAPAAGK
//
