ID A0A242CX38_9ENTE Unreviewed; 423 AA.
AC A0A242CX38;
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=A5875_003988 {ECO:0000313|EMBL:OTO14831.1};
OS Enterococcus sp. 3H8_DIV0648.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1834178 {ECO:0000313|EMBL:OTO14831.1, ECO:0000313|Proteomes:UP000194623};
RN [1] {ECO:0000313|EMBL:OTO14831.1, ECO:0000313|Proteomes:UP000194623}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3H8_DIV0648 {ECO:0000313|EMBL:OTO14831.1,
RC ECO:0000313|Proteomes:UP000194623};
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. 3H8_DIV0648.";
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:OTO14831.1}.
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DR EMBL; NGLG01000002; OTO14831.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A242CX38; -.
DR OrthoDB; 1550290at2; -.
DR Proteomes; UP000194623; 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; TIGR00359; cello_pts_IIC; 1.
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 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 31..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..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..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 222..241
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 329..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 355..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 389..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..410
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000259|PROSITE:PS51105"
SQ SEQUENCE 423 AA; 45961 MW; 95812B07E3A6FA76 CRC64;
MNGFMDKLAE KIMPLANKLG QNRYLTVLRD AFMLSFPLTM FGSIVVVINN LPFFNDATKG
ILGDLFGNGQ NATMSIMSVF VTFGIGYYLS ESYEVEGIFG GAVSFASFLI LTPFAMTLEN
GEKISGILSL DRLGAKGMFI GMIAAFLAAE IYCRVTKRGW QIKMPDGVPP AVTKSFAALI
PAVLTLTVFL IVNAIMTGVF HANLHDVIYE VIQKPLTGLG SSLPATLLAL FLVQFLWFFG
LHGQIIVNSV MDPIWNTLML DNLEAYKAGN PLPHIISKPF METFTVGLGG SGMTLAVVIL
MAFVLKKKQY RDVGRLALAP GIFNVNEPAI FGLPIVLNAT ILIPWVLAPL VVTTINYLVM
AAGIVPPPTG VSVPWTVPIV ASGILATNSW LGGALQVLDF IIVGCIWYPF LRILDRQPNF
DIE
//