ID N1MPW1_9SPHN Unreviewed; 564 AA.
AC N1MPW1;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 51.
DE SubName: Full=PTS system, N-acetylglucosamine-specific IIA component / PTS system, N-acetylglucosamine-specific IIB component / PTS system, N-acetylglucosamine-specific IIC component {ECO:0000313|EMBL:CCW19250.1};
DE EC=2.7.1.69 {ECO:0000313|EMBL:CCW19250.1};
GN ORFNames=EBBID32_36160 {ECO:0000313|EMBL:CCW19250.1};
OS Sphingobium indicum BiD32.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1301087 {ECO:0000313|EMBL:CCW19250.1, ECO:0000313|Proteomes:UP000013201};
RN [1] {ECO:0000313|EMBL:CCW19250.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW19250.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Le V.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCW19250.1, ECO:0000313|Proteomes:UP000013201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BiD32 {ECO:0000313|EMBL:CCW19250.1,
RC ECO:0000313|Proteomes:UP000013201};
RA Nielsen J.L., Zhou N.A., Kjeldal H.;
RT "Bisphenol A degrading Sphingobium sp. strain BiD32.";
RL Submitted (APR-2013) 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:CCW19250.1}.
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DR EMBL; CAVK010000183; CCW19250.1; -; Genomic_DNA.
DR RefSeq; WP_006962440.1; NZ_CAVK010000183.1.
DR AlphaFoldDB; N1MPW1; -.
DR OrthoDB; 7571469at2; -.
DR Proteomes; UP000013201; 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 Reference proteome {ECO:0000313|Proteomes:UP000013201};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCW19250.1};
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 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 201..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 248..274
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..298
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 310..336
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 356..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..389
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 401..483
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT ACT_SITE 423
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 564 AA; 58427 MW; 2168A3C51A154834 CRC64;
MRKIVGSLQP IGRALMLPIA VLPIAGLLLR LGQPDLLGIP LLAAAGDALF SSLGLLFAIG
VATGIARDGN GAAALAGVVC YLVTMHGGRA LIAVPSDVIA GLTDSLAQTV AQAWKARAFA
RLDVPIGIAS GLIGGSLYNR YATISVPAFL SFFGGRRFVP IVAGAAGVGL ALAVGGSYAM
LDAGLDHASH GLVASGHLGL FGFGVINRLL LVTGLHHILN NVAWFVLGDF NGTTGDLRRF
FAGDPHAGAF MAGFFPVMMF GLPAACLAIY RAALPDQKKA VGGMLLSLAL TSFLTGVTEP
IEFSFMFLAP LLYAIHAVLT GIAMVIMDVL GVRLGFGFSA GLFDYLLNFG RATRPWLLLP
VGVAYFLTYY SIFSFAIRRF NLATPGRQPA EAQPDAVTQG GERGAAYLAA LGGSANLQTI
GACTTRLRLV VRDQAGVNDA ALKALGAVAV LRPSAQAVQV IIGPIADQVS EEIRLATTQA
VAPSQIAPVV AEPPASAPVE ARADIVAALG GAEAIVDTRL VAGRLRISLQ RPVDIDALAT
ITDVRGVACI DDRTLHIIGQ DLTR
//
