PTGA_SALTI
ID PTGA_SALTI Reviewed; 169 AA.
AC P0A284; P02908;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=PTS system glucose-specific EIIA component {ECO:0000250|UniProtKB:P69783};
DE AltName: Full=EIIA-Glc {ECO:0000250|UniProtKB:P69783};
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=STY2670, t0424;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(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. The
CC enzyme II complex composed of PtsG and Crr is involved in glucose
CC transport. {ECO:0000250|UniProtKB:P69783}.
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; AL513382; CAD07665.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68142.1; -; Genomic_DNA.
DR RefSeq; NP_456969.1; NC_003198.1.
DR RefSeq; WP_000522253.1; NZ_WSUR01000025.1.
DR PDB; 1O53; NMR; -; A=2-16.
DR PDBsum; 1O53; -.
DR AlphaFoldDB; P0A284; -.
DR BMRB; P0A284; -.
DR SMR; P0A284; -.
DR STRING; 220341.16503651; -.
DR EnsemblBacteria; AAO68142; AAO68142; t0424.
DR GeneID; 64336303; -.
DR GeneID; 67516162; -.
DR KEGG; stt:t0424; -.
DR KEGG; sty:STY2670; -.
DR PATRIC; fig|220341.7.peg.2707; -.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_5_1_6; -.
DR OMA; HTKHAVG; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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 INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT CHAIN 2..169
FT /note="PTS system glucose-specific EIIA component"
FT /id="PRO_0000186534"
FT DOMAIN 39..143
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 91
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P69783,
FT ECO:0000255|PROSITE-ProRule:PRU00416"
FT BINDING 76
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 91
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 76
FT /note="Important for phospho-donor activity"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT MOD_RES 91
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P69783"
FT HELIX 4..11
FT /evidence="ECO:0007829|PDB:1O53"
SQ SEQUENCE 169 AA; 18247 MW; 451098233E8E1479 CRC64;
MGLFDKLKSL VSDDKKDTGT IEIVAPLSGE IVNIEDVPDV VFAEKIVGDG IAIKPTGNKM
VAPVDGTIGK IFETNHAFSI ESDSGIELFV HFGIDTVELK GEGFKRIAEE GQRVKVGDPV
IEFDLPLLEE KAKSTLTPVV ISNMDEIKEL IKLSGSVTVG ETPVIRIKK
