ID   AMYD_THETU              Reviewed;         292 AA.
AC   P37730;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Probable starch degradation products transport system permease protein AmyD;
GN   Name=amyD;
OS   Thermoanaerobacterium thermosulfurigenes (Clostridium thermosulfurogenes).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Thermoanaerobacterium.
OX   NCBI_TaxID=33950;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=DSM 3896 / EM1;
RX   PubMed=1874408; DOI=10.1016/0378-1097(91)90476-q;
RA   Bahl H., Burchhardt G., Wienecke A.;
RT   "Nucleotide sequence of two Clostridium thermosulfurogenes EM1 genes
RT   homologous to Escherichia coli genes encoding integral membrane components
RT   of binding protein-dependent transport systems.";
RL   FEMS Microbiol. Lett. 65:83-87(1991).
CC   -!- FUNCTION: Probably part of a binding-protein-dependent transport system
CC       starch degradation products. Probably responsible for the translocation
CC       of the substrate across the membrane.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC       permease family. MalFG subfamily. {ECO:0000305}.
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DR   EMBL; M57692; AAB00843.1; -; Genomic_DNA.
DR   PIR; S37704; S37704.
DR   AlphaFoldDB; P37730; -.
DR   SMR; P37730; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd06261; TM_PBP2; 1.
DR   Gene3D; 1.10.3720.10; -; 1.
DR   InterPro; IPR000515; MetI-like.
DR   InterPro; IPR035906; MetI-like_sf.
DR   Pfam; PF00528; BPD_transp_1; 1.
DR   SUPFAM; SSF161098; SSF161098; 1.
DR   PROSITE; PS50928; ABC_TM1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..292
FT                   /note="Probable starch degradation products transport
FT                   system permease protein AmyD"
FT                   /id="PRO_0000059948"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        110..130
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          71..281
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ   SEQUENCE   292 AA;  32908 MW;  9FF68F85EED22D8F CRC64;
     MAKKAKFFKN GIWYWLFIAP TLLSLIIVVL IPFIIGIYYS FTDWNGINQP VFIGLKNFMT
     LRDDAEFWNS IIFTAKFAVA CIVIINVVGL SLAMLVTRKI FARNFMRTAF YLPNLIGGLI
     LGFIWNFIFV DVFQTISDAT HIGWLGGWLS TTNTGFWGLV IVTSWQMIGY VMVIYIAYIE
     SIPTDLIEAS KIDGANSWQQ FRNVVFPLIA PAFTVSLFIT LSNSFKLFDQ NLSLTAGAPG
     NTTQMITLNI YQTAFSAQEM AVGQAKAVIM FLIIAVISVI QVYLTQKREV EM