ID A0A1M6D483_PSEXY Unreviewed; 636 AA.
AC A0A1M6D483;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=ATP-binding cassette, subfamily B {ECO:0000313|EMBL:SHI67931.1};
GN ORFNames=SAMN02745725_00845 {ECO:0000313|EMBL:SHI67931.1};
OS Pseudobutyrivibrio xylanivorans DSM 14809.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Pseudobutyrivibrio.
OX NCBI_TaxID=1123012 {ECO:0000313|EMBL:SHI67931.1, ECO:0000313|Proteomes:UP000184185};
RN [1] {ECO:0000313|EMBL:SHI67931.1, ECO:0000313|Proteomes:UP000184185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14809 {ECO:0000313|EMBL:SHI67931.1,
RC ECO:0000313|Proteomes:UP000184185};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQYQ01000004; SHI67931.1; -; Genomic_DNA.
DR RefSeq; WP_072913162.1; NZ_FQYQ01000004.1.
DR AlphaFoldDB; A0A1M6D483; -.
DR STRING; 185007.SAMN02910350_00017; -.
DR OrthoDB; 9762778at2; -.
DR Proteomes; UP000184185; 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:SHI67931.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000184185};
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 28..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 164..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..206
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..309
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 41..331
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000259|PROSITE:PS50929"
FT DOMAIN 397..631
FT /note="ABC transporter"
FT /evidence="ECO:0000259|PROSITE:PS50893"
SQ SEQUENCE 636 AA; 70380 MW; 80982ADD994BE93F CRC64;
MPRGPQPGSV PKLTAEQKAK RRGVLGRLFK YIGANYWLHL IVVVIGIFTA VICNAKGTAF
MQTLIDSYIV PMLKSGSTDF GPLAAAIREL IVYYALGAIA IFVYNYTMIF VGQGTLRSLR
DDMFEKMEDL PIRYFDTHPH GDVMSIYTND IDTMRQMISQ SFPQILNSAI TIVTVFTYMV
LTSWPLTIVT IIMIALITFT TAAVAGRSGS YFRKQQKALG AVNGNIEEIM KGQKVVKVFC
HEDEVMEKFN ELNEELYNNA YKANRLANCI GPVNMQMGNI SYLACAVVGG VLAINGWTGL
TLGGLAAFLQ FNRAFNMPVN QISQQFQSIV LAMAGAERVF DLIDEKPEAD EGYVMLVNAK
EENGEIVECE ERTGMWAWKH YHKAEGTTTY VKLTGDIVFD DVDFSYNPDK PVLHNIKLFA
TPGQKIAFVG ATGAGKTTIT NLINRFYDIA DGKIRYDGIN INKIKKADLR KSLGIVLQDT
HLFTGTIADN IRYGKLDATD EEVVAAAKLA NADSFIHRLP QGYDTVITGD GGNLSQGQRQ
LLAIARAAIA DPPVLILDEA TSSIDTRTEK IVQDGMDKLM HGRTTFVIAH RLSTIRNSDC
IMVLDQGRII ERGSHEELIG EGGKYYQLYT GKIQNA
//
