PTGA_SHIFL
ID PTGA_SHIFL Reviewed; 169 AA.
AC P69785; P08837; Q47703;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 108.
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=SF2472, S2618;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN43979.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17792.1; -; Genomic_DNA.
DR RefSeq; NP_708272.1; NC_004337.2.
DR RefSeq; WP_000522247.1; NZ_WPGW01000027.1.
DR AlphaFoldDB; P69785; -.
DR BMRB; P69785; -.
DR SMR; P69785; -.
DR STRING; 198214.SF2472; -.
DR PRIDE; P69785; -.
DR EnsemblBacteria; AAN43979; AAN43979; SF2472.
DR EnsemblBacteria; AAP17792; AAP17792; S2618.
DR GeneID; 1027210; -.
DR GeneID; 67416817; -.
DR KEGG; sfl:SF2472; -.
DR KEGG; sfx:S2618; -.
DR PATRIC; fig|198214.7.peg.2953; -.
DR HOGENOM; CLU_012312_5_1_6; -.
DR OMA; HTKHAVG; -.
DR OrthoDB; 1481289at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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 3: Inferred from homology;
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_0000186536"
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; 18251 MW; EA18020745531215 CRC64;
MGLFDKLKSL VSDDKKDTGT IEIIAPLSGE IVNIEDVPDV VFAEKIVGDG IAIKPTGNKM
VAPVDGTIGK IFETNHAFSI ESDSGVELFV HFGIDTVELK GEGFKRIAEE GQRVKVGDTV
IEFDLPLLEE KAKSTLTPVV ISNMDEIKEL IKLSGSVTVG ETPVIRIKK
