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Database: UniProt
Entry: A0A2N9JKZ3_9ACTN
LinkDB: A0A2N9JKZ3_9ACTN
Original site: A0A2N9JKZ3_9ACTN 
ID   A0A2N9JKZ3_9ACTN        Unreviewed;       624 AA.
AC   A0A2N9JKZ3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=ABC-type multidrug transport system ATPase and permease component {ECO:0000313|EMBL:SPD88446.1};
GN   ORFNames=MPLG2_3416 {ECO:0000313|EMBL:SPD88446.1};
OS   Micropruina glycogenica.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Micropruina.
OX   NCBI_TaxID=75385 {ECO:0000313|EMBL:SPD88446.1, ECO:0000313|Proteomes:UP000238164};
RN   [1] {ECO:0000313|EMBL:SPD88446.1, ECO:0000313|Proteomes:UP000238164}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1 {ECO:0000313|EMBL:SPD88446.1};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; LT985188; SPD88446.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N9JKZ3; -.
DR   KEGG; mgg:MPLG2_3416; -.
DR   OrthoDB; 9806127at2; -.
DR   Proteomes; UP000238164; Chromosome 1.
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   CDD; cd18550; ABC_6TM_exporter_like; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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:SF658; ABC TRANSPORTER B FAMILY MEMBER 29, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000238164};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        159..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        265..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        290..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..325
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          374..612
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   624 AA;  66705 MW;  C4E604FA0E9607F1 CRC64;
     MSGWQVMNSM TRDSSVRDHR LAPGTRRRVL SYAAAYKGLI AVFLGLTVID SLLVVASPLL
     LQRLIDDGVI PGNAGLVIQL AVLVALIALA DATLTLVERW FSSRIGEGLI YDLRTQVFGH
     VLRQPIAFFT RAQTGALVTR LNSDVIGAQQ AFTSVLQNLV GNAISLVVIV VAMASLSWQL
     TLGALLLVPL FIVPARIIGR RLAGLTRRQM SLNAEMGAQM SERFNVAGAL LVKLFGDPRR
     EDAEYADHAR GVRDVGVTLA VNRSVFFVAL GLVASLATAM VYGFGGVMAV NGLLTVGTLL
     ALAALLARLY APLTALSNVR VDVMTALVSF ERVFEVLDLK PLVEQKPDAV DIPDEPVRVE
     IDQVSFRYPS ADEISLASLE GVASGDRKGS GDILHDITFD VVPGSMVALV GPSGAGKTTI
     TSLVARLYDP TEGAIRVNGV DLRDATLTSL HDRVGVVTQE AHLFHDTLRA NLLYAKPEAT
     TAELEAALRA AQVWHLVESL PAGLDTVVGD RGHRLSGGEK QRFAIARLLL KGPGLVVLDE
     ATAHLDSESE AAVQRALDAA LADRTSIVIA HRLSTVRGAD QILVVDDGRI VERGSHVQLL
     AQGGLYADLY RTQFAEQAVT AAQT
//
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