ID J4UC92_9FIRM Unreviewed; 481 AA.
AC J4UC92;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=PTS system, N-acetylglucosamine-specific IIBC component {ECO:0000313|EMBL:EJP20402.1};
DE EC=2.7.1.69 {ECO:0000313|EMBL:EJP20402.1};
GN Name=nagE {ECO:0000313|EMBL:EJP20402.1};
GN ORFNames=HMPREF1140_0727 {ECO:0000313|EMBL:EJP20402.1};
OS Lachnoanaerobaculum sp. ICM7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Lachnoanaerobaculum.
OX NCBI_TaxID=936594 {ECO:0000313|EMBL:EJP20402.1, ECO:0000313|Proteomes:UP000006599};
RN [1] {ECO:0000313|EMBL:EJP20402.1, ECO:0000313|Proteomes:UP000006599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICM7 {ECO:0000313|EMBL:EJP20402.1,
RC ECO:0000313|Proteomes:UP000006599};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
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:EJP20402.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ALJL01000023; EJP20402.1; -; Genomic_DNA.
DR RefSeq; WP_009663210.1; NZ_ALJL01000023.1.
DR AlphaFoldDB; J4UC92; -.
DR PATRIC; fig|936594.3.peg.1510; -.
DR Proteomes; UP000006599; Unassembled WGS sequence.
DR GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
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:0015572; F:N-acetylglucosamine transmembrane transporter activity; IEA:InterPro.
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 InterPro; IPR010974; PTS_IIBC_nag.
DR NCBIfam; TIGR00826; EIIB_glc; 1.
DR NCBIfam; TIGR01998; PTS-II-BC-nag; 1.
DR PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR30009:SF4; PTS SYSTEM N-ACETYLGLUCOSAMINE-SPECIFIC EIICBA 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 Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EJP20402.1};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 153..172
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 298..322
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..386
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 402..481
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT ACT_SITE 424
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 481 AA; 51051 MW; 9876935B5EF487E6 CRC64;
MKYLQRLGKS LMLPVACLPV AAILMGIGYW IDPTGWGGNN IVAAFLLKAG GAIIDNMAIL
FAIGVAVGMS DDGDGAAALA GLVSWLVITT LLSKGSVAMF TGVEADAVPA AFGKTQTQFI
GIVCGLIGAA CYNKFKTTKL PDALSFFSGK RSVAIVTAGF SLIAAIVLFF IWPLIYGALV
SFGEAILSTG AVGAGIYGFL NRLLIPFGLH HALNSVFWFD VAGINDIGKF WGSAEGGVLG
QTGMYMSGFF PVMMFGLPGA ALAMYHTAKD ARKKAAYGLL LAAALSSFFT GVTEPLEFAF
MFLAPVLYLI HALLTGISLA VVSLLPIRAG FNFSAGLVDW VLSFKAPFAQ NPLLLIPIGV
VYGAIYYAIF RFVITKFDLK TPGREDDEEE EKKAVLANDD FTAVAAIILE GVGGPENLTS
IDNCITRLRL EIKDYTKVDE KKIKSAGVAG VIRPSKTAVQ VIIGTKVQFV ADEFKKLAKN
K
//