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Database: UniProt
Entry: A0A0D7EDX6_RHOPL
LinkDB: A0A0D7EDX6_RHOPL
Original site: A0A0D7EDX6_RHOPL 
ID   A0A0D7EDX6_RHOPL        Unreviewed;       920 AA.
AC   A0A0D7EDX6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Multidrug ABC transporter ATP-binding protein {ECO:0000313|EMBL:KIZ38948.1};
GN   ORFNames=OO17_21960 {ECO:0000313|EMBL:KIZ38948.1};
OS   Rhodopseudomonas palustris.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=1076 {ECO:0000313|EMBL:KIZ38948.1, ECO:0000313|Proteomes:UP000032515};
RN   [1] {ECO:0000313|EMBL:KIZ38948.1, ECO:0000313|Proteomes:UP000032515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BAL398 {ECO:0000313|EMBL:KIZ38948.1,
RC   ECO:0000313|Proteomes:UP000032515};
RA   Bentzon-Tilia M., Severin I., Hansen L.H., Riemann L.;
RT   "Genomics and ecophysiology of heterotrophic nitrogen fixing bacteria
RT   isolated from estuarine surface water.";
RL   Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in beta-(1-->2)glucan export. Transmembrane domains
CC       (TMD) form a pore in the inner membrane and the ATP-binding domain
CC       (NBD) is responsible for energy generation.
CC       {ECO:0000256|ARBA:ARBA00024722}.
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}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily.
CC       {ECO:0000256|ARBA:ARBA00005417}.
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:KIZ38948.1}.
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DR   EMBL; JXXE01000479; KIZ38948.1; -; Genomic_DNA.
DR   RefSeq; WP_044415606.1; NZ_JXXE01000479.1.
DR   AlphaFoldDB; A0A0D7EDX6; -.
DR   STRING; 1421013.GCA_000504425_03497; -.
DR   PATRIC; fig|1076.23.peg.5165; -.
DR   OrthoDB; 9805029at2; -.
DR   Proteomes; UP000032515; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd03230; ABC_DR_subfamily_A; 2.
DR   Gene3D; 3.40.1710.10; abc type-2 transporter like domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR047651; ABC2_perm_RbbA.
DR   InterPro; IPR013525; ABC2_TM.
DR   InterPro; IPR047817; ABC2_TM_bact-type.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; NF033858; ABC2_perm_RbbA; 1.
DR   PANTHER; PTHR43038; ATP-BINDING CASSETTE, SUB-FAMILY H, MEMBER 1; 1.
DR   PANTHER; PTHR43038:SF4; RIBOSOME-ASSOCIATED ATPASE; 1.
DR   Pfam; PF12698; ABC2_membrane_3; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51012; ABC_TM2; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:KIZ38948.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        568..588
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        722..748
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        775..795
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        807..826
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        893..915
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..248
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          278..508
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   DOMAIN          688..918
FT                   /note="ABC transmembrane type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51012"
SQ   SEQUENCE   920 AA;  99217 MW;  F3BD1FB806609D53 CRC64;
     MSDGTTAVAA PVARLDAVGQ RYGTSIALEA ITLDLPAGCM VGLIGPDGVG KSTLLALLAG
     ARVIRTGSVT VLGADMADAA QRRRTCPRIA YMPQGLGKNL YPTLSVFENV DFFGRLFGHD
     KRERTRRIQQ LLQKTGLAPF ADRPAGKLSG GMKQKLGLCC ALIHDPDLLI LDEPTTGVDP
     LSRRQFWQLI DEIRAGRAGM SVVVATAYME EAAGFDWLVA MNAGRVLATG APADLLRQTG
     AATLDAAFIA MLPERDRQGY AEVVIPPRVA AADAGIAIEA EHLTMRFDGF TAVDDVSFRI
     ARGEIFGFLG SNGCGKTTTM KMLTGLLPAS EGRARLFGNE VDPNDMNVRR RVGYMSQGFS
     LYSELTVRQN LELHARLFQM EPAAIPARIV EMTQRFDLGE VIDSLPDPLP LGVRQRLSLA
     VAMIHSPDIL ILDEPTSGVD PVARDGFWQI LSDLSRKDSV TIFISTHFMN EAERCDRISL
     MHAGRVLVSD APAAIVAARS AETLEQAFIA YLQDAIGQPA PASAGVVALP EPGPAAGAAA
     VRGRRLFDLR RMLAYSRREA LELRRDPIRA TLATIGSVIL LFVLGYGINL DVEKLSFAAL
     DRDDTTISRD YILQIAGSRY FKEGDPIADY ADLDRRMRSG RLTVAVEIPP GFGRDVAHGR
     DVQIGVWIDG AMPARAETAR GYVQAMHQSW LTQKARELYG AAATAGSFQI ALRYRYNPGI
     KSLVAMAPAV IPLLLLMIPA MLAVLSVVRE KELGSIINFY TTPVTRLEFL IGKQIPYIVL
     AMLNAILLAA FAILVFRVPF TGSPMTFLAG ALLYVTIATS MGLVLSTFMS SQIAAIFGTA
     LLTLIPAIQF SGLTDPVSSL QGFGAMIGRI YPTTYFINIT RGTFSKALGF ADLAGSFLPL
     LVAIPILLGL GVVLLKKQAD
//
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