PTGA_MYCCT
ID PTGA_MYCCT Reviewed; 154 AA.
AC P45618; Q2SSP2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=PTS system glucose-specific EIIA component {ECO:0000303|PubMed:7703858};
DE AltName: Full=EIIA-Glc {ECO:0000303|PubMed:7703858};
DE AltName: Full=EIII-Glc {ECO:0000250|UniProtKB:P69783};
DE AltName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P69783};
GN Name=crr; OrderedLocusNames=MCAP_0234;
OS Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343
OS / NCTC 10154).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=340047;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=7703858; DOI=10.1002/pro.5560031125;
RA Zhu P.-P., Reizer J., Peterkofsky A.;
RT "Unique dicistronic operon (ptsI-crr) in Mycoplasma capricolum encoding
RT enzyme I and the glucose-specific enzyme IIA of the
RT phosphoenolpyruvate:sugar phosphotransferase system: cloning, sequencing,
RT promoter analysis, and protein characterization.";
RL Protein Sci. 3:2115-2128(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=California kid / ATCC 27343 / NCTC 10154;
RA Glass J.I., Lartigue C., Pfannkoch C., Baden-Tillson H., Smith H.O.,
RA Venter J.C., Roske K., Wise K.S., Calcutt M.J., Nelson W.C., Nierman W.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=9705652; DOI=10.1016/s0969-2126(98)00072-0;
RA Huang K., Kapadia G., Zhu P.-P., Peterkofsky A., Herzberg O.;
RT "A promiscuous binding surface: crystal structure of the IIA domain of the
RT glucose-specific permease from Mycoplasma capricolum.";
RL Structure 6:697-710(1998).
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. The
CC enzyme II complex composed of PtsG and Crr is involved in glucose
CC transport. {ECO:0000250|UniProtKB:P69783, ECO:0000305|PubMed:7703858}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:P69783};
CC Note=Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion
CC is important for dimerization. {ECO:0000250|UniProtKB:P69783};
CC -!- SUBUNIT: Heterodimer with glycerol kinase (glpk).
CC {ECO:0000250|UniProtKB:P69783}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
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; U15110; AAA70407.1; -; Genomic_DNA.
DR EMBL; CP000123; ABC01309.1; -; Genomic_DNA.
DR RefSeq; WP_011387122.1; NC_007633.1.
DR PDB; 2GPR; X-ray; 2.50 A; A=1-154.
DR PDBsum; 2GPR; -.
DR AlphaFoldDB; P45618; -.
DR SMR; P45618; -.
DR EnsemblBacteria; ABC01309; ABC01309; MCAP_0234.
DR GeneID; 23778813; -.
DR KEGG; mcp:MCAP_0234; -.
DR HOGENOM; CLU_012312_5_1_14; -.
DR OMA; HTKHAVG; -.
DR OrthoDB; 1481289at2; -.
DR PhylomeDB; P45618; -.
DR EvolutionaryTrace; P45618; -.
DR Proteomes; UP000001928; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 2.70.70.10; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR TIGRFAMs; TIGR00830; PTBA; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Kinase; Metal-binding; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transport; Zinc.
FT CHAIN 1..154
FT /note="PTS system glucose-specific EIIA component"
FT /id="PRO_0000186542"
FT DOMAIN 26..130
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 78
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P69783,
FT ECO:0000255|PROSITE-ProRule:PRU00416"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with glycerol kinase"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared with glycerol kinase"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT SITE 63
FT /note="Important for phospho-donor activity"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT MOD_RES 78
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT STRAND 8..11
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:2GPR"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2GPR"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 36..48
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 53..57
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:2GPR"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:2GPR"
FT HELIX 112..118
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2GPR"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:2GPR"
SQ SEQUENCE 154 AA; 16703 MW; F5C90163FBB01B70 CRC64;
MWFFNKNLKV LAPCDGTIIT LDEVEDEVFK ERMLGDGFAI NPKSNDFHAP VSGKLVTAFP
TKHAFGIQTK SGVEILLHIG LDTVSLDGNG FESFVTQDQE VNAGDKLVTV DLKSVAKKVP
SIKSPIIFTN NGGKTLEIVK MGEVKQGDVV AILK
