PTGA_SALTY
ID PTGA_SALTY Reviewed; 169 AA.
AC P0A283; P02908;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=PTS system glucose-specific EIIA component {ECO:0000303|PubMed:6086327};
DE AltName: Full=EIIA-Glc {ECO:0000303|PubMed:6086327};
DE AltName: Full=EIII-Glc {ECO:0000303|PubMed:6086327};
DE AltName: Full=Glucose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:6754734};
GN Name=crr; OrderedLocusNames=STM2433;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6086327; DOI=10.1002/j.1460-2075.1984.tb02015.x;
RA Nelson S.O., Schuitema A.R.J., Benne R., van der Ploeg L.H.T.,
RA Plijter J.S., Aan F., Postma P.W.;
RT "Molecular cloning, sequencing, and expression of the crr gene: the
RT structural gene for IIIGlc of the bacterial PEP:glucose phosphotransferase
RT system.";
RL EMBO J. 3:1587-1593(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=789369; DOI=10.1016/s0021-9258(17)32988-5;
RA Saier M.H. Jr., Roseman S.;
RT "Sugar transport. The crr mutation: its effect on repression of enzyme
RT synthesis.";
RL J. Biol. Chem. 251:6598-6605(1976).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6754734; DOI=10.1016/s0021-9258(19)45410-0;
RA Meadow N.D., Roseman S.;
RT "Sugar transport by the bacterial phosphotransferase system. Isolation and
RT characterization of a glucose-specific phosphocarrier protein (IIIGlc) from
RT Salmonella typhimurium.";
RL J. Biol. Chem. 257:14526-14537(1982).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=6292227; DOI=10.1016/s0021-9258(19)45412-4;
RA Stock J.B., Waygood E.B., Meadow N.D., Postma P.W., Roseman S.;
RT "Sugar transport by the bacterial phosphotransferase system. The glucose
RT receptors of the Salmonella typhimurium phosphotransferase system.";
RL J. Biol. Chem. 257:14543-14552(1982).
RN [6]
RP FUNCTION.
RX PubMed=17158705; DOI=10.1128/mmbr.00024-06;
RA Deutscher J., Francke C., Postma P.W.;
RT "How phosphotransferase system-related protein phosphorylation regulates
RT carbohydrate metabolism in bacteria.";
RL Microbiol. Mol. Biol. Rev. 70:939-1031(2006).
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 (PubMed:6754734, PubMed:6292227). It can also phosphorylate
CC mannose, methyl alpha-glucoside and 2-deoxy-glucose (PubMed:6292227).
CC The non-phosphorylated EIII-Glc is an inhibitor for uptake of certain
CC sugars such as maltose, melibiose, lactose, and glycerol.
CC Phosphorylated EIII-Glc, however, may be an activator for adenylate
CC cyclase (PubMed:789369). {ECO:0000269|PubMed:6292227,
CC ECO:0000269|PubMed:6754734, ECO:0000269|PubMed:789369,
CC ECO:0000305|PubMed:17158705}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 uM for methyl alpha-glucoside (with phospho-IIIGlc Slow)
CC {ECO:0000269|PubMed:6754734};
CC KM=6 uM for methyl alpha-glucoside {ECO:0000269|PubMed:6292227};
CC KM=10 uM for glucose {ECO:0000269|PubMed:6292227};
CC KM=40 uM for mannose {ECO:0000269|PubMed:6292227};
CC KM=200 uM for 2-deoxy-glucose {ECO:0000269|PubMed:6292227};
CC Vmax=126 umol/min/mg enzyme with methyl alpha-glucoside as substrate
CC {ECO:0000269|PubMed:6292227};
CC Vmax=126 umol/min/mg enzyme with glucose as substrate
CC {ECO:0000269|PubMed:6292227};
CC Vmax=10 umol/min/mg enzyme with mannose as substrate
CC {ECO:0000269|PubMed:6292227};
CC Vmax=10 umol/min/mg enzyme with 2-deoxy-glucose as substrate
CC {ECO:0000269|PubMed:6292227};
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}.
CC -!- DISRUPTION PHENOTYPE: In mutants defective in enzyme I and histidine-
CC containing phosphate carrier protein (HPr), cells lacking this gene are
CC able to grow on the non-PTS compounds such as glycerol, maltose,
CC melibiose, mannose 6-phosphate, and alpha-glycerol phosphate.
CC {ECO:0000269|PubMed:789369}.
CC -!- MISCELLANEOUS: Two forms of III-Glc (called IIIGlc Slow and IIIGlc
CC Fast) are present in living cells. IIIGlc Fast, derived from IIIGlc
CC Slow by cleavage of the seven NH2-terminal amino acids, is present only
CC in trace quantities and has slight activity (only 2-3% of phospho-
CC IIIGlc Slow) in the phosphorylation of sugar. Both forms accept
CC phosphate from phosphoenolpyruvate via Enzyme I and HPr, however only
CC IIIGlc Slow participates in the phosphorylation of glucose or methyl
CC alpha-D-glucoside. IIIGlc Fast may play a role in the regulation of
CC non-PTS sugar transport systems. {ECO:0000269|PubMed:6754734}.
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DR EMBL; X05210; CAA28837.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL21327.1; -; Genomic_DNA.
DR PIR; A03405; WQEB3T.
DR RefSeq; NP_461368.1; NC_003197.2.
DR RefSeq; WP_000522253.1; NC_003197.2.
DR AlphaFoldDB; P0A283; -.
DR BMRB; P0A283; -.
DR SMR; P0A283; -.
DR IntAct; P0A283; 1.
DR STRING; 99287.STM2433; -.
DR PaxDb; P0A283; -.
DR EnsemblBacteria; AAL21327; AAL21327; STM2433.
DR GeneID; 1253955; -.
DR GeneID; 64336303; -.
DR GeneID; 67516162; -.
DR KEGG; stm:STM2433; -.
DR PATRIC; fig|99287.12.peg.2571; -.
DR HOGENOM; CLU_012312_5_1_6; -.
DR OMA; HTKHAVG; -.
DR PhylomeDB; P0A283; -.
DR BioCyc; SENT99287:STM2433-MON; -.
DR PRO; PR:P0A283; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
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 Cytoplasm; Kinase; Metal-binding; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW 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_0000186535"
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"
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
