AMYC_THETU
ID AMYC_THETU Reviewed; 274 AA.
AC P37729; P26828;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 25-MAY-2022, entry version 82.
DE RecName: Full=Probable starch degradation products transport system permease protein AmyC;
GN Name=amyC;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 115-274.
RC STRAIN=DSM 3896 / EM1;
RX PubMed=1854207; DOI=10.1128/aem.57.5.1554-1559.1991;
RA Bahl H., Burchhardt G., Spreinat A., Haeckel K., Wienecke A., Schmidt B.,
RA Antranikian G.;
RT "Alpha-amylase of Clostridium thermosulfurogenes EM1: nucleotide sequence
RT of the gene, processing of the enzyme, and comparison of other alpha-
RT amylases.";
RL Appl. Environ. Microbiol. 57:1554-1559(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; AAB00844.1; -; Genomic_DNA.
DR PIR; S37705; S37705.
DR AlphaFoldDB; P37729; -.
DR SMR; P37729; -.
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..274
FT /note="Probable starch degradation products transport
FT system permease protein AmyC"
FT /id="PRO_0000059947"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 73..93
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 69..259
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT CONFLICT 115..155
FT /note="IPFQSVMIPLVAEFGKFHFLTRSGLVFMYLGFGSSLGVFLY -> DPVSISY
FT DSISSGIWEISFSYKVRACIYVLGIWFKLRSVFIL (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 274 AA; 30994 MW; 5921E22D0A4B8819 CRC64;
MRKVHVQKYL LTFLGIVLSL LWISPFYIIL VNSFKTKLEL FTNTLSLPKS LMLDNYKTAA
ANLNLSEAFS NTLIITVFSI LIIAIFSSMT AYALQRVKRK SSVIIYMIFT VAMLIPFQSV
MIPLVAEFGK FHFLTRSGLV FMYLGFGSSL GVFLYYGALK GIPTSLDEAA LIDGCSRFRI
YWNIILPLLN PTTITLAVLD IMWIWNDYLL PSLVINKVGS RTLPLMIFYF FSQYTKQWNL
GMAGLTIAIL PVVIFYFLAQ RKLVTAIIAG AVKQ