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Database: UniProt
Entry: A0A1H3FJP9_9FIRM
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ID   A0A1H3FJP9_9FIRM        Unreviewed;       584 AA.
AC   A0A1H3FJP9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:SDX91065.1};
GN   ORFNames=SAMN02910414_00257 {ECO:0000313|EMBL:SDX91065.1};
OS   Lachnobacterium bovis DSM 14045.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Lachnobacterium.
OX   NCBI_TaxID=1122142 {ECO:0000313|EMBL:SDX91065.1, ECO:0000313|Proteomes:UP000183918};
RN   [1] {ECO:0000313|EMBL:SDX91065.1, ECO:0000313|Proteomes:UP000183918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14045 {ECO:0000313|EMBL:SDX91065.1,
RC   ECO:0000313|Proteomes:UP000183918};
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; FNPG01000005; SDX91065.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3FJP9; -.
DR   STRING; 1122142.SAMN02910414_00257; -.
DR   Proteomes; UP000183918; 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; cd18547; ABC_6TM_Tm288_like; 1.
DR   CDD; cd03254; ABCC_Glucan_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; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF499; FATTY ACID ABC TRANSPORTER ATP-BINDING_PERMEASE PROTEIN; 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:SDX91065.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183918};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        20..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        69..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        248..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          25..312
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          346..579
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   584 AA;  65597 MW;  A75979C1CC5B3A0D CRC64;
     MEEYKFSESI KKLIHYCRKY YFPMIFAFML SIFGTAFNII GPDKLKEITN KISEGIITNV
     MDVDGILKII TVLVTLYILG FLFNTSQGVI MASCTQRITN KMRKDISFKI NKIPLKYFDQ
     TTVGNTLSRV TNDVDTIGQS LNQSIGTLIS GITMFFGSLI MMTKTNWIMT VAGVLATIFG
     FLIMMLITKK SQKYFALQQE ELGRLNGLIE ETYTGHNVIA AYNDVHKEIE NFHEINNRLY
     SSAWKSQFLS GLMMPLMTFI GNLGYVAVCV TGAILVEKDM TEIGTIVAFM MYIRLFTQPL
     AQMAQAITSL QATAAASGRV FEFLAEEELE DESCKNVEIK DFKGHIEFEH VSFGYTSEKT
     IINDFNLNVK PGEKVAIVGP TGAGKSTLVN LLMRFYEINQ GTIRIDGVDI KDLRREQVHE
     LFGMVLQDTW LFEGTIKDNI RYNMSSVSDE DVINASKAVG LDKYVKALPE LYDTVLNDKT
     TLSAGQKQLI TIARAYVMNA PMLILDEATS SVDTRTELII QRAMDKLSEG RTCFVIAHRL
     STIKNADTIL VLNNGDIIES GNHKQLLEKG GFYADLYNSQ FDIA
//
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