ID   A0A109IMF1_9ACTN        Unreviewed;      1203 AA.
AC   A0A109IMF1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=ABC-type multidrug transport system, ATPase and permease component {ECO:0000313|EMBL:SCG54360.1};
GN   ORFNames=GA0070623_2238 {ECO:0000313|EMBL:SCG54360.1};
OS   Micromonospora rifamycinica.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG54360.1, ECO:0000313|Proteomes:UP000198226};
RN   [1] {ECO:0000313|EMBL:SCG54360.1, ECO:0000313|Proteomes:UP000198226}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG54360.1,
RC   ECO:0000313|Proteomes:UP000198226};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LT607752; SCG54360.1; -; Genomic_DNA.
DR   RefSeq; WP_067304916.1; NZ_LT607752.1.
DR   AlphaFoldDB; A0A109IMF1; -.
DR   OrthoDB; 9806127at2; -.
DR   Proteomes; UP000198226; Chromosome i.
DR   GO; GO:0016020; C: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   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 2.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR011527; ABC1_TM_dom.
DR   InterPro; IPR036640; ABC1_TM_sf.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR039421; Type_1_exporter.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS50929; ABC_TM1F; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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        46..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        150..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        231..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        266..285
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        666..689
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        701..721
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        775..792
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   1203 AA;  126302 MW;  01C85C8F4498E201 CRC64;
     MRLLRDLWAS APRRVSVVIV LVVLGAAGQA AASAVAGPVL VHRSAGWFVA LVVALVVAVF
     SELVIALLMA GITADWSADV RRRLCRVALG QDLPTLEGTP VGELLDRIDN DVYQVAAELR
     NTGVRLIQGL VLCLLAAVSA LFVWWPAGVA MLLLTALLGV LLRRPTAAIT PARMAEEEAW
     SDLAAVMEEA VHGQDDVRTS LAQPYVLRLF ARRAAEVLSR CRRVFLMSAR VTAFAAGVIR
     IGIAGVVLAG AWALTTGRVD GARLTAIWLL ALSFGATVEH LARWVPHLQY ALGAWARVLL
     LSDSRQEPSG GVTPTDGDLT LRGLTFRYPA AQGERGPALR DVRLSFVRGR SYALVGRTGS
     GKSTLAKVLT RAVEVPRGTV LLGDTDLCDL DVEELRRWIA VVPQRTEILA GTLAENVALF
     DPDLLDAAPR ALAELGLTGW VAELPDGIRT RLGEGGYVLS AGQEQLVAFA RILVRDPHVV
     ILDEATARLD PVTEIRVREA TERLLTDRIG IIIAHRLSSV QRCDEVVVMA DGAVLEAGPL
     RSSARFAELL ATSRAAAYTP AGTARGGVGL LDGPAPTCPD GDGEEWKAGG AVRGSQGPAT
     GEAVGEAVRG SAGQATGEAG ATGGGAGAAG GRAVVVPKRD PPPLPPAAPA RTMGEILRLA
     VNDPRFGLLS VAMFVVMSVL GLDGTVLPWL WADVVDGGSP WLPAIGIVGA LLVVLPLPYW
     TNLRFPQWWV RQMLRMSLRL VHGQTGARRT STHTPAEVVA QSGDTERVVQ LADNLMDQFI
     AVIIMVVMTA VTGSPVPGLF FLGTMAVSGL AATLFGPRLE RSARDTVAAR AAFATALVSS
     LSAARTVKLA GATRPVLDHL SALDLVRSDR QRREIAAQVW ARSTPSVVSG LLPIGAWALY
     LAGGLSAGAT LVAVSTLGAA RWFAWTTAAL VSQYPSARVW TRRTVAMTGV GAYSAKVPGV
     DLVAGTAPAP EPPPRRPLRR LELAGFGALH SDGTLAVREV DLTVDRGQLV LVVGPVGAGK
     SSLLRALAGI VHHVGELRWN GQPVTEPELF LRPGQVGYVG QLPRVLSGTV ADNIALGHDV
     DAAGAVTTAQ LTPDLAAGGG LGLLIGHKGT RLSGGQLQRL ALARALAPRT ELLVADDVSS
     ALDVTTELAL WAALREHGVT VVGSTAKRAA LVRADHVVVL VDGTVAAQGP WRDLENDWGH
     LAG
//