ID A0A239V708_9MICO Unreviewed; 689 AA.
AC A0A239V708;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=EIICBA-Glc {ECO:0000313|EMBL:SNV17842.1};
GN Name=ptsG_1 {ECO:0000313|EMBL:SNV17842.1};
GN ORFNames=SAMEA4475696_00305 {ECO:0000313|EMBL:SNV17842.1};
OS Dermatophilus congolensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermatophilaceae;
OC Dermatophilus.
OX NCBI_TaxID=1863 {ECO:0000313|EMBL:SNV17842.1, ECO:0000313|Proteomes:UP000242637};
RN [1] {ECO:0000313|EMBL:SNV17842.1, ECO:0000313|Proteomes:UP000242637}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13039 {ECO:0000313|EMBL:SNV17842.1,
RC ECO:0000313|Proteomes:UP000242637};
RG Pathogen Informatics;
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; LT906453; SNV17842.1; -; Genomic_DNA.
DR RefSeq; WP_028327317.1; NZ_LT906453.1.
DR AlphaFoldDB; A0A239V708; -.
DR STRING; 1121387.GCA_000429885_01410; -.
DR GeneID; 63458602; -.
DR KEGG; dco:SAMEA4475696_0305; -.
DR OrthoDB; 9797715at2; -.
DR Proteomes; UP000242637; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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 NCBIfam; TIGR00826; EIIB_glc; 1.
DR NCBIfam; TIGR00830; PTBA; 1.
DR PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE 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; 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:UP000242637};
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 24..44
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 131..150
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..218
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 225..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 263..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 296..313
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 319..341
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 373..395
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..407
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 426..507
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 560..665
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000259|PROSITE:PS51093"
FT REGION 404..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 407..422
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 506..527
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 448
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 689 AA; 73307 MW; CED95619CF830F1E CRC64;
MSTTTDTAPS RAPRKGRFSG LQRFAKSLML PIALLPAAGL LLRFGQEDVL GWIETPVVSP
FFDAMTAAGD SIFKQLAILF AVGIAIGMAK KADGSTALAA VAGYIVIESV FKAMSPVVLA
GKVDIAGEPL TINYGVLGGI VVGLITAKLF DRFHDIELPT YLGFFGGRRF VPIVVSFTVL
IVGFAMSYCY PLFNAGLTTL ATGIASAGAV GAFLYGLFNR LLIPFGLHHI INIYIWFQYG
SFATPDGALH GELTRFASGD PTAGILTSGF YPILMFGLPG AALAMMHCAR PNQKKFAAGI
FGAAGLTAFL TGITEPLEFA FMFAAFPLYV LHAILTGLSL AAAYTLDIHL GFSFSAGLID
LLLYGNSKAA HNIPLLVGLG VGFFVLYYVV FRFAITAWNL RTPGREDTTS GDSEKEEQNS
ASTDRNEMAT QLVEAFGGRE NLLYVDACIT RLRIEVENTS LVNKERLREL GAAGVLEVGN
NIQAVFGPRA ESLKHDMRQV LTGEETPVSE KENTSSHDAA PSNKKSDATP DSGEKDTATD
ELIIFAPITG RVVPLSEVPD ETFSDGLLGN GLAIEPEEKT KIPVTAPVSG ELVQMWPHAF
VIKTPSGRKI LTHLGIETVG LKGKGFTKHA NAGDTVEAGQ LLIDYDVAAV AKSGRNVVVP
VMALETSPEA IAKPATGQVE GADPLYTVR
//
