ID A0A0M2H769_9MICO Unreviewed; 643 AA.
AC A0A0M2H769;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=PTS system glucose-specific EIICBA component {ECO:0000313|EMBL:KJL39779.1};
GN Name=ptsG {ECO:0000313|EMBL:KJL39779.1};
GN ORFNames=RS82_03986 {ECO:0000313|EMBL:KJL39779.1};
OS Microbacterium trichothecenolyticum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=69370 {ECO:0000313|EMBL:KJL39779.1, ECO:0000313|Proteomes:UP000034098};
RN [1] {ECO:0000313|EMBL:KJL39779.1, ECO:0000313|Proteomes:UP000034098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8608 {ECO:0000313|EMBL:KJL39779.1,
RC ECO:0000313|Proteomes:UP000034098};
RA Corretto E.;
RT "Draft genome sequences of ten Microbacterium spp. with emphasis on heavy
RT metal contaminated environments.";
RL Submitted (FEB-2015) 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:KJL39779.1}.
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DR EMBL; JYJA01000041; KJL39779.1; -; Genomic_DNA.
DR RefSeq; WP_045302646.1; NZ_JYJA01000041.1.
DR AlphaFoldDB; A0A0M2H769; -.
DR PATRIC; fig|69370.6.peg.4046; -.
DR OrthoDB; 9797715at2; -.
DR Proteomes; UP000034098; 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; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
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; TIGR00830; PTBA; 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; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 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:UP000034098};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..199
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 211..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..265
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..289
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 350..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..383
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 403..485
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 530..634
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT ACT_SITE 425
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 643 AA; 68324 MW; FDB0AFC566C35E16 CRC64;
MKFLQRLGRS IMLPVAVLPV AAILVGISNW IKGTIGGGVV VDFLYTAGIS LLSNLALLFA
VGISIGMAKK SDGTSALAGV VSWLVVTTLL KPESVMLFMG VNDVNEVPAA FANVENVFVG
ILCGLIGAFC YDRFKDTKLP DALSFFSGKR SVAIVTAGFS LVLAAILFFV WPFVYGGLVT
FGEWISFLGP LGAGIYGFLN RLLIPIGLHH ALNSVFWFDV AGINDLNNFL AGTGTYGVTG
QYMTGFFPIM MFGLPGAALA MYLTAKSTRK KITYGILLSA AIASFFVGVT EPLEFSFMFL
APVLYLVHAV FTGISMAISA ILPVRMGFGF SAGFVDLVLN WTNPMAQNPW LIPVMGVFWF
FIYFGVFYFF IKRFNLKTPG REDDNILEEG TEFDTHDVDQ KYLVTGSRFI DALGGKENIL
DLDNCATRLR LEIDDVSQVD DAALKRAGAA GTMKPGGKSV QVIYGTNVQF VKDAMEQIIS
GQAEAPAGAA PEQTPATGGT AVLTDAPTTT AVKLRQPLEG KIVPLTAVPD PTFAQGIMGP
GVAIEPTGDT VVAPADGTIG ATFDSSHAVA LVLGDGTELL IHVGIDTVGM KGDGFETLVE
KGQKVTAGTP LLRFDLAKIH AAGHPSITPV IVLNNENAAV TFE
//
