PTG3C_MYCPN
ID PTG3C_MYCPN Reviewed; 940 AA.
AC P75569;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=PTS system glucose-specific EIICBA component {ECO:0000250|UniProtKB:Q57071};
DE EC=2.7.1.199 {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=EII-Glc/EIII-Glc;
DE AltName: Full=EIICBA-Glc {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=EIICBA-Glc 1 {ECO:0000305};
DE Includes:
DE RecName: Full=Glucose permease IIC component {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=PTS system glucose-specific EIIC component {ECO:0000250|UniProtKB:Q57071};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=PTS system glucose-specific EIIB component {ECO:0000250|UniProtKB:Q57071};
DE Includes:
DE RecName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:Q57071};
DE AltName: Full=PTS system glucose-specific EIIA component {ECO:0000250|UniProtKB:Q57071};
GN Name=ptsG; OrderedLocusNames=MPN_207; ORFNames=MP624;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (sugar PTS), a major carbohydrate active transport system,
CC catalyzes the phosphorylation of incoming sugar substrates
CC concomitantly with their translocation across the cell membrane. This
CC system is involved in glucose transport.
CC {ECO:0000250|UniProtKB:Q57071}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC glucose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:33367,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4167,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:61548, ChEBI:CHEBI:64837;
CC EC=2.7.1.199; Evidence={ECO:0000250|UniProtKB:Q57071};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC cysteinyl or histidyl residue, depending on the transported sugar.
CC Then, it transfers the phosphoryl group to the sugar substrate
CC concomitantly with the sugar uptake processed by the EIIC domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00416}.
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DR EMBL; U00089; AAB96272.1; -; Genomic_DNA.
DR PIR; S73950; S73950.
DR RefSeq; NP_109895.1; NC_000912.1.
DR RefSeq; WP_010874564.1; NC_000912.1.
DR AlphaFoldDB; P75569; -.
DR SMR; P75569; -.
DR IntAct; P75569; 4.
DR STRING; 272634.MPN_207; -.
DR PRIDE; P75569; -.
DR EnsemblBacteria; AAB96272; AAB96272; MPN_207.
DR KEGG; mpn:MPN_207; -.
DR PATRIC; fig|272634.6.peg.226; -.
DR HOGENOM; CLU_012312_1_1_14; -.
DR OMA; AWAFNRF; -.
DR BioCyc; MPNE272634:G1GJ3-335-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; -; 1.
DR Gene3D; 3.30.1360.60; -; 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 Pfam; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 2.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00830; PTBA; 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; PS51103; PTS_EIIC_TYPE_1; 1.
PE 3: Inferred from homology;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..940
FT /note="PTS system glucose-specific EIICBA component"
FT /id="PRO_0000186560"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 83..103
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 175..195
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 487..507
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 515..535
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 537..557
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 564..584
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 598..618
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..284
FT /note="PTS EIIC type-1; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 479..630
FT /note="PTS EIIC type-1; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 661..743
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 794..907
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT REGION 285..478
FT /note="Unknown"
FT ACT_SITE 683
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 847
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ SEQUENCE 940 AA; 101619 MW; 44B836307FDA36EF CRC64;
MQIKAQDTGQ QKKSCLLSNI RNKWKNRNRG SFRQWVGKLS NGLMIPIAVL PIAGIFLGVG
DAIAGNAGDL TGLRYFGLFI KNGGDVVFAN LPILFAIAIA ITFSQDAGVA GFSAFVFWAA
MNGFMSSLIL PFDKAGKIIT DTSTPIAGFK VLYNKSVPVH AIATTLGLRT LSTSVFGGII
VGALTSVLYK KFYAIRLPDV IGFFSGTRFV PIICFVVAIP VALILLMIWP AVSIGLNAIG
TGLGFLGGKG YGANSLIFGY IERSLIPFGV HHAFYAPLWY TSAGGSLQEI VNQQVWIRPD
FHLSDNYVAR VIGWVDPNNS SMYIIPGALN GQNGSSTGNT MSKDLNGALS AYMSKESTAF
LTWKDLVDGL TFKGNFDKMA ENGLLDGSNK IWLGLNGSGI LGKKLLLSDG NVYTITFKTF
ANTTPIAWSK GAQAVLPLNA SSTIVNNPTA LAAATQSNNN TNNIKLYPVN SFRVAVESLN
PAQYSQGKFP FMLFGIPAAG VAMILAAPKD RRKEAASIVG SAAFTSFLTG ITEPFEFTFL
FLAPWLFYGV HAVLAAVSFW LMNILGANVG QTFSGSFIDF ILYGALPDGR RWLANSYLVP
IIGLFLAAIY FPTFYFLIKH FNLATPGRGG KLITKKEYLA SKAAAKAEGV SGVAENFTQT
QIEAGILLQA YGGKENIVEL GACITKLRVT VKNPELVKEE PIKELGAAGV MRTTPTFFVA
VFGTRAAVYK SAMQDIIQGK VNWEALQKVI NTDQLAVEPK ETTPPKEVMP VVQDEIVILS
PVNGTLKSLN QVPDETFKQK LVGEGVAIVP SDGHFKAPGE AGVKTELAFP GGHAYIFDID
GIKVMLHIGI DTVQINAKKQ PGEPLEVFDI KTKQGEYTKE KSESVVEVDL KKLSKKYNPI
TPFVVMKESL ENFKLVPIRQ RGEIKVGQPI FKLVYKKSQA
