ID A0A0S8IAL1_9CHLR Unreviewed; 363 AA.
AC A0A0S8IAL1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Transport permease protein {ECO:0000256|RuleBase:RU361157};
GN ORFNames=AMJ88_05375 {ECO:0000313|EMBL:KPK94129.1};
OS Anaerolineae bacterium SM23_ 63.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK94129.1, ECO:0000313|Proteomes:UP000051685};
RN [1] {ECO:0000313|EMBL:KPK94129.1, ECO:0000313|Proteomes:UP000051685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK94129.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU361157};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU361157}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ABC-2 integral membrane protein family.
CC {ECO:0000256|RuleBase:RU361157}.
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:KPK94129.1}.
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DR EMBL; LJUS01000011; KPK94129.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8IAL1; -.
DR Proteomes; UP000051685; Unassembled WGS sequence.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-UniRule.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR Gene3D; 3.40.1710.10; abc type-2 transporter like domain; 1.
DR InterPro; IPR013525; ABC2_TM.
DR InterPro; IPR047817; ABC2_TM_bact-type.
DR InterPro; IPR000412; ABC_2_transport.
DR PANTHER; PTHR43027; DOXORUBICIN RESISTANCE ABC TRANSPORTER PERMEASE PROTEIN DRRC-RELATED; 1.
DR PANTHER; PTHR43027:SF2; TRANSPORT PERMEASE PROTEIN; 1.
DR Pfam; PF12698; ABC2_membrane_3; 1.
DR PRINTS; PR00164; ABC2TRNSPORT.
DR PROSITE; PS51012; ABC_TM2; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|RuleBase:RU361157};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU361157};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU361157};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU361157}; Transport {ECO:0000256|RuleBase:RU361157}.
FT TRANSMEM 21..40
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 172..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 281..302
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT TRANSMEM 338..360
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU361157"
FT DOMAIN 134..363
FT /note="ABC transmembrane type-2"
FT /evidence="ECO:0000259|PROSITE:PS51012"
SQ SEQUENCE 363 AA; 39441 MW; EB3713659C324929 CRC64;
MKAITALYLA QAREFLRDRS AVLFVLLLPV VFGVFFGLVF SEGGSFTLQL GLANEDPGPM
GAQIVMNLDA PEAKGGYNVF TGEREELMTI LKRGDLHALL VLPENLSQSV MNGQSALIEV
FYDTANPTSA DFAVSIVRTL LNEINLALSG SPPILEMAPQ PVQTKPTRSI DFFMPGMLGV
ALLWLGIFGT AQPIVSQRET QILRRIGVTP VSRLTILTAE VSWRVTVGLL QAPVFLLVGY
FGFGVGVISW PPFIGAIVLG TLVFVSLGYV LAGLGRSTES VMAISQLINF PMMMLSGSIF
MVEMLPDLFK PIMSALPLTY LSDLLRQSMV GATAMHPIGL DFAVLGGWLV VLFILAVKLW
RWE
//