ID A0A242K0J9_9ENTE Unreviewed; 454 AA.
AC A0A242K0J9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Permease IIC component {ECO:0000256|PIRNR:PIRNR006351};
GN ORFNames=A5844_001239 {ECO:0000313|EMBL:OTP11105.1};
OS Enterococcus sp. 10A9_DIV0425.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1987383 {ECO:0000313|EMBL:OTP11105.1, ECO:0000313|Proteomes:UP000194933};
RN [1] {ECO:0000313|EMBL:OTP11105.1, ECO:0000313|Proteomes:UP000194933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=10A9_DIV0425 {ECO:0000313|EMBL:OTP11105.1,
RC ECO:0000313|Proteomes:UP000194933};
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. 10A9_DIV0425.";
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:OTP11105.1}.
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DR EMBL; NGMO01000002; OTP11105.1; -; Genomic_DNA.
DR RefSeq; WP_002319286.1; NZ_NGMO01000002.1.
DR AlphaFoldDB; A0A242K0J9; -.
DR STRING; 1987383.A5844_001239; -.
DR Proteomes; UP000194933; 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:SF4; PTS SYSTEM N,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIC 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 Reference proteome {ECO:0000313|Proteomes:UP000194933};
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 34..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..168
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 301..320
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 400..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..427
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000259|PROSITE:PS51105"
SQ SEQUENCE 454 AA; 49532 MW; 7FCB5A91B8B032C0 CRC64;
MSFMDKFQSA IERLLVPLST KLNAQRHICA VRDAFILSFP LTMAGSLMVL LNNVFLSADG
FMFKILQFDK LFPGIVKFQA VFAPVVKGSA DIFSILIVFL IARNLAKLME GDDLLTGLTA
ISVYFIIYPD YFDNEGVNYL TNQYMGAQGL FVAILVGLLV GELMSRLAKS DKLEIKMPEQ
VPPAVARSFK VLIPIIITTI FFSVLNYFVK MAAPGGLHEL IYNIIQTPLT RMSQSLFSVI
ILALLSQLLW AMGIHGPNTI AAIRDTMFSE AGNANLLHYA ESGTTWGAPY PITYSGLATA
FAEYGGSGAT LGLIIAILIF SKNKESKSIG KLSFVPGLFN INEMVIFGLP IILNPIYIIP
FIIAPLVNIM IGYTAVMILK IMPPVTIGIP WTTPGPLMPF LGTGGNIVAL FVGFICLAVS
VLIYSPFVIA ANKAAIIEDE MENEIQSQEV VESI
//
