ID A0A242ARK5_9ENTE Unreviewed; 422 AA.
AC A0A242ARK5;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE RecName: Full=Permease IIC component {ECO:0000256|PIRNR:PIRNR006351};
GN ORFNames=A5821_003299 {ECO:0000313|EMBL:OTN83376.1};
OS Enterococcus sp. 7F3_DIV0205.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834189 {ECO:0000313|EMBL:OTN83376.1, ECO:0000313|Proteomes:UP000194948};
RN [1] {ECO:0000313|EMBL:OTN83376.1, ECO:0000313|Proteomes:UP000194948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7F3_DIV0205 {ECO:0000313|EMBL:OTN83376.1,
RC ECO:0000313|Proteomes:UP000194948};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genomic Center for Infectious Diseases;
RA Earl A., Manson A., Schwartman J., Gilmore M., Abouelleil A., Cao P.,
RA Chapman S., Cusick C., Shea T., Young S., Neafsey D., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus sp. 7F3_DIV0205.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (PTS), a major carbohydrate active -transport system, catalyzes
CC the phosphorylation of incoming sugar substrates concomitant with their
CC translocation across the cell membrane.
CC {ECO:0000256|PIRNR:PIRNR006351}.
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:OTN83376.1}.
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DR EMBL; NGKX01000002; OTN83376.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242ARK5; -.
DR STRING; 1834189.A5821_003299; -.
DR OrthoDB; 1550290at2; -.
DR Proteomes; UP000194948; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR004501; PTS_EIIC_3.
DR InterPro; IPR004796; PTS_IIC_cello.
DR NCBIfam; TIGR00410; lacE; 1.
DR PANTHER; PTHR33989; -; 1.
DR PANTHER; PTHR33989:SF8; PERMEASE IIC COMPONENT; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR PIRSF; PIRSF006351; PTS_EIIC-Cellobiose; 1.
DR PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR006351};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006351};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW ECO:0000256|PIRNR:PIRNR006351};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006351}.
FT TRANSMEM 28..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..89
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 138..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 236..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 336..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 363..380
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..405
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000259|PROSITE:PS51105"
SQ SEQUENCE 422 AA; 46177 MW; 10D85628D457C0C6 CRC64;
MKKKLIGLFD KVSPFFDKMG NNPYLQAISG AMMSTLGPVF IGSIAVLLVV FMNMSKTLQE
FTQVIALLGK VNTFTIGSLA LYISVLMAIN LVRKLDEKED YVAAGIISLM SFLLITPLDK
TADEIAALPT TWLSAQGVFS AMIVGLVVGR LFIAIKRKGW TIKMPEGVPP MVTRMFESLI
PTVLIGILFI LVDLGFSLTA FGNMHQFVYT IIQEPLKGIG GSIGAMIILS LIQQILWFFG
IHGTNVILPL VTPLWMAMDV ENMNAVTAGQ TPPNIVGLAF FNIITFGGMA LGLVLLMLRA
KSKQYREVGK ISIVPALFGI TEPVIFGTPL VLNFDLAVPF IFNNSIGLIL AYVLTKIGLV
SKFVGVQAIF GLPVGFHAAV QGSISVIILQ LVIQLVLSPL LWYPWFKRLD KKTYLREQSE
EV
//
