ID A0A0N0E5W2_9PSED Unreviewed; 580 AA.
AC A0A0N0E5W2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=PTS system, N-acetylglucosamine-specific IIBC component {ECO:0000313|EMBL:KPA92926.1};
GN ORFNames=PF66_00667 {ECO:0000313|EMBL:KPA92926.1};
OS Pseudomonas fuscovaginae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=50340 {ECO:0000313|EMBL:KPA92926.1, ECO:0000313|Proteomes:UP000037931};
RN [1] {ECO:0000313|EMBL:KPA92926.1, ECO:0000313|Proteomes:UP000037931}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IRRI 6609 {ECO:0000313|EMBL:KPA92926.1,
RC ECO:0000313|Proteomes:UP000037931};
RX PubMed=26422147;
RA Quibod I.L., Grande G., Oreiro E.G., Borja F.N., Dossa G.S., Mauleon R.,
RA Cruz C.V., Oliva R.;
RT "Rice-Infecting Pseudomonas Genomes Are Highly Accessorized and Harbor
RT Multiple Putative Virulence Mechanisms to Cause Sheath Brown Rot.";
RL PLoS ONE 10:E0139256-E0139256(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00421}.
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:KPA92926.1}.
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DR EMBL; JSYZ01000002; KPA92926.1; -; Genomic_DNA.
DR RefSeq; WP_054061881.1; NZ_JSYZ01000002.1.
DR AlphaFoldDB; A0A0N0E5W2; -.
DR STRING; 50340.PF66_00667; -.
DR PATRIC; fig|50340.43.peg.2674; -.
DR OrthoDB; 7571469at2; -.
DR Proteomes; UP000037931; 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; 2.
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; 2.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; Glucose permease domain IIB; 2.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 2.
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..67
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..114
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..250
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..359
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..371
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 384..467
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 484..567
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT ACT_SITE 406
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 580 AA; 61690 MW; 47900D6277700EF6 CRC64;
MYQLFIEGLQ RLGRALMLPI AILPIAGLLL RLGDADLLDI AIIHDAGNAI FTNLALIFAI
GIAVGFARDN NGTAGLAGVI GYLVLVATLK VIDAEINMGM LAGIISGLLG GALYNRFKDI
KLPEYLAFFG GRRFVPIVTG FSAVGLGLVF GLIWPPIQHG INSLGLMMVE SGSIGAFIFG
VFNRLLIVTG LHHILNNMMW FVFGSFTDPD TGRVVTGDLA RYFAGDPRAG QFMTGMFPVM
VFGLPAACLA MYRNALPERR KLMGGILLSM ALTSFLTGVT EPIEFAFMFL APLLYVVHAL
LTGLSMAITN LLDIHLGFTF SGGAIDMALG WGKSTNGWLV LPVGLAYAAI YYAVFDFCIR
RFDLKTPGRE IIANPATNQT LDDSQRAAAY IRALGGADNL LTVGACTTRL RLELRDRDKA
LDSELKELGA LAVVRPGQGG SLQVVVGPLA DGIADEIRLA LPNTATHLPA ASAPVAAEVN
GISPGQLQQW LDALGGRENV LALDCVAQTR LRVQLEDVDK LSEAQLSALG CKGISPLTGG
AWHLLIGVQA AGVGEALRAT LRSRPDARPH TPAFRRDGSA
//