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Database: UniProt
Entry: F2JGA8_CELLD
LinkDB: F2JGA8_CELLD
Original site: F2JGA8_CELLD 
ID   F2JGA8_CELLD            Unreviewed;       452 AA.
AC   F2JGA8;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=PTS system, glucose-like IIB subunint {ECO:0000313|EMBL:ADZ81803.1};
DE            EC=2.7.1.69 {ECO:0000313|EMBL:ADZ81803.1};
GN   OrderedLocusNames=Clole_0041 {ECO:0000313|EMBL:ADZ81803.1};
OS   Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS   RHM5) (Clostridium lentocellum).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC   Cellulosilyticum.
OX   NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ81803.1, ECO:0000313|Proteomes:UP000008467};
RN   [1] {ECO:0000313|EMBL:ADZ81803.1, ECO:0000313|Proteomes:UP000008467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC   {ECO:0000313|Proteomes:UP000008467};
RX   PubMed=21398547; DOI=10.1128/JB.00239-11;
RG   US DOE Joint Genome Institute;
RA   Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA   Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA   Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA   Angert E.R., Currie C.R.;
RT   "Complete genome sequence of the cellulose-degrading bacterium
RT   Cellulosilyticum lentocellum.";
RL   J. Bacteriol. 193:2357-2358(2011).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP002582; ADZ81803.1; -; Genomic_DNA.
DR   AlphaFoldDB; F2JGA8; -.
DR   STRING; 642492.Clole_0041; -.
DR   KEGG; cle:Clole_0041; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_012312_2_0_9; -.
DR   Proteomes; UP000008467; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0103111; F:D-glucosamine PTS permease activity; IEA:UniProtKB-EC.
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   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   PANTHER; PTHR30175:SF7; NEGATIVE REGULATOR OF SACY ACTIVITY; 1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 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:UP000008467};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADZ81803.1};
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        112..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        145..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        218..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        249..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        358..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..419
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        426..446
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          120..452
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   452 AA;  47949 MW;  9E6DB30B56E52525 CRC64;
     MDYKQAALKV LEGIGGKDNL VSGAHCATRL RLVLADNSHL NKKANEAVDG VKGVFEAQGQ
     VQIIFGTGIV NKVFDEFSKA AKIETATKEE VKQVAIAKIS PFKRAIKTLG DVFVPIIPDI
     VASGLLMGLL EGLGKVFPSL AAADTFTLLS LFDNVAFVFL PILIAISTAK VFSGNLFLGA
     VIGMIMIHPN LINAWNVAGM ESIPQFSVWF GLYDIGQVGY QGHVIPIVIS VCFMSKLEKK
     LHQFVPEVID LFVTPLITVL VTGYLALTVI GSVFAFAENW VLVGVQWLIA IPFGIGSFLM
     GGAYAKTVVS GVHHMYNVIE AGMISADGIN TWMPIASVAN VAQGAVALKV RDKKIKALTI
     LASLSAFLGI TEPAIFGVNI RYMKPFIAGS IGGACGALVA SIFNVGATAY GVTGIFGFLI
     TTNSAFGYLL TLVVAASVAF VISWVLGVDE NR
//
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