ID L0M0B0_ENTBF Unreviewed; 444 AA.
AC L0M0B0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Permease IIC component {ECO:0000256|PIRNR:PIRNR006351};
GN OrderedLocusNames=D782_1341 {ECO:0000313|EMBL:AGB77354.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB77354.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB77354.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB77354.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
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}.
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DR EMBL; CP003938; AGB77354.1; -; Genomic_DNA.
DR AlphaFoldDB; L0M0B0; -.
DR STRING; 693444.D782_1341; -.
DR KEGG; ebf:D782_1341; -.
DR PATRIC; fig|693444.3.peg.1281; -.
DR eggNOG; COG1455; Bacteria.
DR HOGENOM; CLU_029688_1_2_6; -.
DR OrthoDB; 5843984at2; -.
DR Proteomes; UP000011002; Chromosome.
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:UP000011002};
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..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..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 300..321
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 396..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..426
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000259|PROSITE:PS51105"
SQ SEQUENCE 444 AA; 48188 MW; BE06522C733F78A4 CRC64;
MSLMDSFERG MEKVLVPVAI KLNSQIHVSA IRDAFILSFP IVMASSLIIL INFAILSPDG
FIASLLHLGA LFPNLADAQQ IFTPVMNGSV SIMSILITFL VARNIAIQYR QDDLLCGLTA
IGAFFVVYTP YKVIDGQTYL TTKFLGPQGL FVAVIVALIA SEIFCRLARN PKVTIAMPDA
VPPAVARSFK VLLPIFFVMI LFSVMNYLLT KISPNGLNDL IYTLIQAPLK DMGTNIVTVL
ILGLVSNFLW VIGIHGPNTV AAIRETIFSE ANLENLSYAA SHGTTWGAPY PITWVGINDA
FANCGGSGMT LGLLLAIFIA SHRQDYRDMA KMAFVPGLFN INEPVMFGLP VVLNPILIIP
FVLVPFINSL IGYFFIVMEF IPPMAYAVPW TTPGPLIAFF ASGGNWLALL VGVLCLGVST
LVYLPFVIAA NKVNISAATQ SENE
//
