PTN3B_CORGL
ID PTN3B_CORGL Reviewed; 683 AA.
AC Q46072;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=PTS system mannose-specific EIIBCA component;
DE AltName: Full=EII-Man/EIII-Man;
DE AltName: Full=EIIBCA-Man;
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.191;
DE AltName: Full=PTS system mannose-specific EIIB component;
DE Includes:
DE RecName: Full=Mannose permease IIC component;
DE AltName: Full=PTS system mannose-specific EIIC component;
DE Includes:
DE RecName: Full=Mannose-specific phosphotransferase enzyme IIA component;
DE AltName: Full=PTS system mannose-specific EIIA component;
GN Name=ptsM; Synonyms=ptsG; OrderedLocusNames=Cgl1360, cg1537;
OS Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS JCM 1318 / LMG 3730 / NCIMB 10025).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8039653; DOI=10.1111/j.1574-6968.1994.tb06880.x;
RA Lee J.K., Sung M.H., Yoon K.H., Yu J.H., Oh T.K.;
RT "Nucleotide sequence of the gene encoding the Corynebacterium glutamicum
RT mannose enzyme II and analyses of the deduced protein sequence.";
RL FEMS Microbiol. Lett. 119:137-145(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA Ikeda M., Nakagawa S.;
RT "The Corynebacterium glutamicum genome: features and impacts on
RT biotechnological processes.";
RL Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 10025;
RX PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT impact on the production of L-aspartate-derived amino acids and vitamins.";
RL J. Biotechnol. 104:5-25(2003).
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 mannose transport.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannose(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannose 6-phosphate(in) + L-histidyl-[protein]; Xref=Rhea:RHEA:49232,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:4208,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:58735, ChEBI:CHEBI:64837;
CC EC=2.7.1.191;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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 -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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.
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DR EMBL; L18874; AAA53546.1; -; Genomic_DNA.
DR EMBL; BA000036; BAB98753.1; -; Genomic_DNA.
DR EMBL; BX927152; CAF21369.1; -; Genomic_DNA.
DR RefSeq; NP_600576.1; NC_003450.3.
DR RefSeq; WP_011014304.1; NC_006958.1.
DR AlphaFoldDB; Q46072; -.
DR SMR; Q46072; -.
DR STRING; 196627.cg1537; -.
DR KEGG; cgb:cg1537; -.
DR KEGG; cgl:Cgl1360; -.
DR PATRIC; fig|196627.13.peg.1327; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_2_1_11; -.
DR OMA; PMGVWNF; -.
DR BRENDA; 2.7.1.191; 960.
DR BRENDA; 2.7.1.199; 960.
DR Proteomes; UP000000582; 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; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF55604; SSF55604; 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; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 4: Predicted;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..683
FT /note="PTS system mannose-specific EIIBCA component"
FT /id="PRO_0000186645"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 260..280
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 409..429
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 442..462
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..89
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 117..476
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 550..654
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 28
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 602
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ SEQUENCE 683 AA; 72571 MW; 0B42CAEC60828075 CRC64;
MASKLTTTSQ HILENLGGPD NITSMTHCAT RLRFQVKDQS IVDQQEIDSD PSVLGVVPQG
STGMQVVMGG SVANYYQEIL KLDGMKHFAD GEATESSSKK EYGGVRGKYS WIDYAFEFLS
DTFRPILWAL LGASLIITLL VLADTFGLQD FRAPMDEQPD TYVFLHSMWR SVFYFLPIMV
GATAARKLGA NEWIGAAIPA ALLTPEFLAL GSAGDTVTVF GLPMVLNDYS GQVFPPLIAA
IGLYWVEKGL KKIIPEAVQM VFVPFFSLLI MIPATAFLLG PFGIGVGNGI SNLLEAINNF
SPFILSIVIP LLYPFLVPLG LHWPLNAIMI QNINTLGYDF IQGPMGAWNF ACFGLVTGVF
LLSIKERNKA MRQVSLGGML AGLLGGISEP SLYGVLLRFK KTYFRLLPGC LAGGIVMGIF
DIKAYAFVFT SLLTIPAMDP WLGYTIGIAV AFFVSMFLVL ALDYRSNEER DEARAKVAAD
KQAEEDLKAE ANATPAAPVA AAGAGAGAGA GAAAGAATAV AAKPKLAAGE VVDIVSPLEG
KAIPLSEVPD PIFAAGKLGP GIAIQPTGNT VVAPADATVI LVQKSGHAVA LRLDSGVEIL
VHVGLDTVQL GGEGFTVHVE RRQQVKAGDP LITFDADFIR SKDLPLITPV VVSNAAKFGE
IEGIPADQAN SSTTVIKVNG KNE
