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Database: UniProt
Entry: A0A416JS60_9FIRM
LinkDB: A0A416JS60_9FIRM
Original site: A0A416JS60_9FIRM 
ID   A0A416JS60_9FIRM        Unreviewed;       587 AA.
AC   A0A416JS60;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   SubName: Full=ABC transporter ATP-binding protein {ECO:0000313|EMBL:RHQ15724.1};
GN   ORFNames=DW974_11185 {ECO:0000313|EMBL:RHQ15724.1};
OS   Lachnospiraceae bacterium AM48-27BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX   NCBI_TaxID=2292271 {ECO:0000313|EMBL:RHQ15724.1, ECO:0000313|Proteomes:UP000285913};
RN   [1] {ECO:0000313|EMBL:RHQ15724.1, ECO:0000313|Proteomes:UP000285913}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM48-27BH {ECO:0000313|EMBL:RHQ15724.1,
RC   ECO:0000313|Proteomes:UP000285913};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RHQ15724.1}.
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DR   EMBL; QUFC01000020; RHQ15724.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A416JS60; -.
DR   Proteomes; UP000285913; 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; cd18548; ABC_6TM_Tm287_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:SF276; ABC TRANSPORTER, ATP-BINDING_PERMEASE PROTEIN; 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:RHQ15724.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000285913};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        52..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        157..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        242..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          16..298
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS50929"
FT   DOMAIN          339..574
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000259|PROSITE:PS50893"
SQ   SEQUENCE   587 AA;  64407 MW;  B6547233BE733B68 CRC64;
     MKKLLKYLKD YKLESVMGPL FKMLEASFEL FVPLVMANII DTGIKNADQP YIWKMCGMLI
     LLAAIGLTCS LTAQYFSAKA AVGFGTALRN DLFRHINSLS YREIDTIGTS TLITRMTSDI
     NQVQSGVNLV LRLFLRSPFI VFGAMIMAFQ VNVRAALIFV VAIPLLSIVV FGILLISMPL
     YKKVQKQLDR VLLTTRENLL GARVVRAFNR QQDEMKKFDE ENSLLVNSQV FVGKISALMN
     PVTYVIVNGA TIILIWTGAW QVEGGIITQG AVVALVNYMS QILVELVKLA NLIITISKSL
     ACANRISAVF EETSSIEDKA DAAVLAANAG DAKEQPAKVE FASMDFAYAG SSENALSQIS
     FQAMRGQTIG IIGGTGSGKS TLVNLIPRFY DATGGMVLVD GVNVKDMPLQ ALREKIGIVP
     QKAVLFKGTL RDNIRWGKSD ATDEEIYHAL EIAQARDFVD GKDEGLDLMI QQGGKNLSGG
     QKQRLTIARA LVRNPEILVL DDSASALDFA TDAALRKAIR ENTKDMTVFL VSQRATTIKN
     ADQILVLDDG NLVGRGTHKE LLDTCEVYRE ICFSQLSEKE VREHAEA
//
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