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Database: UniProt
Entry: D4K1I4_9FIRM
LinkDB: D4K1I4_9FIRM
Original site: D4K1I4_9FIRM 
ID   D4K1I4_9FIRM            Unreviewed;       480 AA.
AC   D4K1I4;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=Phosphotransferase system IIC components, glucose/maltose/N-acetylglucosamine-specific {ECO:0000313|EMBL:CBL00133.1};
GN   ORFNames=FP2_28580 {ECO:0000313|EMBL:CBL00133.1};
OS   Faecalibacterium prausnitzii L2-6.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=718252 {ECO:0000313|EMBL:CBL00133.1, ECO:0000313|Proteomes:UP000008804};
RN   [1] {ECO:0000313|EMBL:CBL00133.1, ECO:0000313|Proteomes:UP000008804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Faecalibacterium prausnitzii L2/6.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL00133.1, ECO:0000313|Proteomes:UP000008804}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-6 {ECO:0000313|Proteomes:UP000008804};
RA   Pajon A.;
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; FP929045; CBL00133.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4K1I4; -.
DR   STRING; 718252.FP2_28580; -.
DR   KEGG; fpr:FP2_28580; -.
DR   PATRIC; fig|718252.3.peg.1039; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_012312_2_0_9; -.
DR   BioCyc; FPRA718252:G1375-2454-MONOMER; -.
DR   Proteomes; UP000008804; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF3; PTS SYSTEM N-ACETYLMURAMIC ACID-SPECIFIC EIIBC COMPONENT; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008804};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBL00133.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        121..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        154..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        226..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        309..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..396
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        416..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        450..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..87
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          116..480
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   ACT_SITE        26
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   480 AA;  50321 MW;  39435D5F42A6E5E9 CRC64;
     MTNEELVRAA LEKVGGKSNV LTATNCMTRL RVRVKDDAKI DDDGLKAIEG VMGIVHDRTG
     YVEIVVGPGK CRKCADICRD MGIPADAAAS TANDWQTNKA AVKAGQKQSK VRELFKTFGD
     IFIPLIPGVV ASGLCAGINS LIGQVVPNYA DIPALALIST LLGLMNTCFL GYLTAWVGYR
     AAEKFGGTPI LGGMLGMITG LDGINKISSI LGLFNEAVPL DSILRAGRGG VLAVVLGAWC
     LVKIERWVRK WMPESLDIVF TPLITMILCL VPYILVIMPA TGYVSTALCW VVEKLCMSDV
     LIVRIIAGYV STALFLPMVA MGMHHGLVAL YSVQLESFGY VTLYPALAMA GAGQVGAAVA
     IYFKAKKCGN TRLKNVITGA LPAGLLGIGE PLIYGVTLPM GKPFISAGLG AGFGGAFVMA
     MQVAATAWGP SGLLALFVMT AGPHGVAASV GCYAVGLVIC YIMGFIVTNA MVSVEDVANA
//
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