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Database: UniProt
Entry: I9LIQ3_9FIRM
LinkDB: I9LIQ3_9FIRM
Original site: I9LIQ3_9FIRM 
ID   I9LIQ3_9FIRM            Unreviewed;       477 AA.
AC   I9LIQ3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   SubName: Full=PTS system, N-acetylglucosamine-specific IIBC subunit {ECO:0000313|EMBL:EIW20389.1};
GN   ORFNames=FB4_2353 {ECO:0000313|EMBL:EIW20389.1};
OS   Pelosinus fermentans B4.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Pelosinus.
OX   NCBI_TaxID=1149862 {ECO:0000313|EMBL:EIW20389.1, ECO:0000313|Proteomes:UP000004324};
RN   [1] {ECO:0000313|EMBL:EIW20389.1, ECO:0000313|Proteomes:UP000004324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4 {ECO:0000313|EMBL:EIW20389.1,
RC   ECO:0000313|Proteomes:UP000004324};
RX   PubMed=22933770; DOI=10.1128/JB.01174-12;
RA   Brown S.D., Podar M., Klingeman D.M., Johnson C.M., Yang Z.K.,
RA   Utturkar S.M., Land M.L., Mosher J.J., Hurt R.A.Jr., Phelps T.J.,
RA   Palumbo A.V., Arkin A.P., Hazen T.C., Elias D.A.;
RT   "Draft Genome Sequences for Two Metal-Reducing Pelosinus fermentans Strains
RT   Isolated from a Cr(VI)-Contaminated Site and for Type Strain R7.";
RL   J. Bacteriol. 194:5147-5148(2012).
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:EIW20389.1}.
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DR   EMBL; AKVJ01000007; EIW20389.1; -; Genomic_DNA.
DR   RefSeq; WP_007931209.1; NZ_AKVJ01000007.1.
DR   AlphaFoldDB; I9LIQ3; -.
DR   PATRIC; fig|1149862.3.peg.633; -.
DR   OrthoDB; 9764327at2; -.
DR   Proteomes; UP000004324; 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: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};
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        15..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        95..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        227..249
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        312..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..357
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..369
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          383..464
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   ACT_SITE        405
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   477 AA;  51162 MW;  FC1E185D486B763E CRC64;
     MGNWFGKLQK IGKALMLPVA VLPAAALLLR FGAPDVLDIP FVMKAGGAIF DNLALLFAMG
     IAIGLSHDNG GASGLSGAIG YLVLTNGLKT INPDLNMSVL GGILSGLVAG YLYNRFYNIK
     LPDFLGFFAG RRFVPIVTAA AGIVMAGIFG VIWAPIQSII HSMGEWIIGA GSLGLFVYGI
     FNRLLIPFGL HHILNSFVWF VFGNYTDATG KVVTGDLNRF FAGDPTAGGF MAGFYLIFMF
     ALPAAALAIY TCAKPENRSK IGGALLSVGF TAFLTGITEP IEFMFMFLAP MLYFLHAIMT
     GLAMALVSSM GILHGFGFSA GLIDLLLNWG LATKPAMLVP LGLGFAALYY VVFVWAIKQF
     NIPTPGRFDD EAENTKLDNV DSSDFSMNLI EKLGGAENIE VVDSCITRLR LTLKNAALLD
     ENEMKALGAA GVIKSGNSVQ IIVGTKAEMI ADEMKKLLIE RRNHITKDIH NTSTPNF
//
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