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Database: UniProt
Entry: A0A1I2JCH5_9MICO
LinkDB: A0A1I2JCH5_9MICO
Original site: A0A1I2JCH5_9MICO 
ID   A0A1I2JCH5_9MICO        Unreviewed;       640 AA.
AC   A0A1I2JCH5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:SFF51543.1};
GN   ORFNames=SAMN05216329_1147 {ECO:0000313|EMBL:SFF51543.1};
OS   Curtobacterium sp. YR515.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Curtobacterium.
OX   NCBI_TaxID=1855316 {ECO:0000313|EMBL:SFF51543.1, ECO:0000313|Proteomes:UP000199282};
RN   [1] {ECO:0000313|EMBL:SFF51543.1, ECO:0000313|Proteomes:UP000199282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YR515 {ECO:0000313|EMBL:SFF51543.1,
RC   ECO:0000313|Proteomes:UP000199282};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOOD01000002; SFF51543.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2JCH5; -.
DR   Proteomes; UP000199282; Unassembled WGS sequence.
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; cd18546; ABC_6TM_Rv0194_D2_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, ECO:0000313|EMBL:SFF51543.1};
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        79..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        124..149
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        202..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        225..241
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        300..324
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..366
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          400..634
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  69088 MW;  2907417ACDAF0C52 CRC64;
     MSQQEKNLPV DTSAGPGGAD PVVDDIADTQ AAAPVTASIT TLGVRGEERE DFTKAESRRL
     RRRSLALLGS LAAPLKARLV VLAVVVVVST AGTVAGPALI AWGIDNALPA VMEQNDWVPA
     FGVVATYIVV AVLGAVLTAW YTVLAARISQ AILFDLRKRV FLHTQRLSLE FHETYTSGRI
     ISRQTSDLDS IRELLDSGLN QLIQGVLYMV FTAIALVALD PTSGLVLAVS LVPLWFLIRW
     FQSNSQTLFR ATRVTSARVI VHFVETMTGI RAVQAFRKES RNRDEYGGYV EDYRQANTKV
     FNLFGTFDPV LVLIGNVTLA AVVVVGGFRI VGGTLEVGAL LAVALYAKRF FDPAQELAMF
     YNGYQSASAA MEKISGVLEE RPSVPDPAKP VKLPDATGKM DFDDVVFAYN KGKVVLPEFD
     LHIPAGQTIA LVGSTGAGKS TLAKLMARFY DPSQGSVKLD GVDLRDLDTK DMRRAIVMVT
     QEAYLFSGTV ADNIALGKPG ASRSEIESAA KAVGAHEFIM ALPDGYDTDV NKRGGRVSAG
     QRQLLSFARA FIADPKVLIL DEATASLDIP SERLVQEGLE TLLADRTAVI IAHRLSTVAI
     AHRVLVMEYG RIVEDGTPDD LIAGTGRFAQ LHAAWRDSLV
//
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