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Database: UniProt
Entry: A0A1G8TCH7_9FIRM
LinkDB: A0A1G8TCH7_9FIRM
Original site: A0A1G8TCH7_9FIRM 
ID   A0A1G8TCH7_9FIRM        Unreviewed;       778 AA.
AC   A0A1G8TCH7;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:SDJ39208.1};
GN   ORFNames=SAMN04487760_10628 {ECO:0000313|EMBL:SDJ39208.1};
OS   Lachnospiraceae bacterium G41.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=1200749 {ECO:0000313|EMBL:SDJ39208.1, ECO:0000313|Proteomes:UP000199016};
RN   [1] {ECO:0000313|EMBL:SDJ39208.1, ECO:0000313|Proteomes:UP000199016}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G41 {ECO:0000313|EMBL:SDJ39208.1,
RC   ECO:0000313|Proteomes:UP000199016};
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; FNEU01000006; SDJ39208.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G8TCH7; -.
DR   STRING; 1200749.SAMN04487760_10628; -.
DR   OrthoDB; 9762778at2; -.
DR   Proteomes; UP000199016; 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   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:SDJ39208.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199016};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        200..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        326..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        353..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        441..462
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..499
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          533..767
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   778 AA;  87165 MW;  1561672AA57B9F73 CRC64;
     MKDNKLTKNI LNKIKEYKIH ESDILSVCPI DLSFEGEYIL GYIFLTKDYL GVCESDIPSG
     YTHFFRGTKV HKKDEDEDLA EYEVKLFDLK KIEHIHVERM IGAVLLSAEY DGSPMKIASL
     TNTYLEQLNL FVRHTKNIKN GKDFDADIVG KEAEEEDEEL LYCPICGTMY PDPAKKVCPK
     CTNKRTIFAR VLKYFFKYRF SIAILFLSYA LGAAISVVWP YLTGKVLFDH ILEKDSEYLA
     TFGLAGKFTL ALGLLALIMI GSRIIEEITN VVQMALMARV ATSTVNDIKT DVFSAMSRLS
     LNFFTSKQTG GLMTRVLSDS NRVTEFFIDG IPSVFIHGIT IIITFVVMYR LNWQMALIAC
     ILLPLLVFMT VKLRPGLWNL SGKRHRAEKA VSSKANDNLT GARVVKAFGQ EDAEIERFTN
     PNNNLKDAEI NIVKLRNKFT ILYSLVQEIS SIWIWIIGVF FVLKTDKIDL GVLLTFVGYV
     AHLNGPMNFF SRVFRMWSES INAAQRLFEI IDSIPEIVEK ENPVRLMKPR GEIELSNVTF
     GYTVSRNVLK NINLKVKEGE VLGIVGRSGA GKSTLVNLIS RLYDVKEGSI KIDGVDVKDL
     SLSDLRKNVA MVSQDTYIFM GSVAKNIAYG NENATGEEII RAAKLAGAHD FISKMPDGYD
     TVIGASGKDL SGGEKQRISI ARAILADPKI LILDEATASV DTETEKAIQN SLKLLVKGRT
     TLSIAHRLST LRDADRLIVI DNGRIVEEGT HAELDKNEDG IFHKLNELQN KSLAVTNF
//
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