ID   PTGA_BUCAP              Reviewed;         167 AA.
AC   Q8KA51;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
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=BUsg_060;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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   -!- 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; AE013218; AAM67631.1; -; Genomic_DNA.
DR   RefSeq; WP_011053597.1; NC_004061.1.
DR   AlphaFoldDB; Q8KA51; -.
DR   SMR; Q8KA51; -.
DR   STRING; 198804.BUsg_060; -.
DR   EnsemblBacteria; AAM67631; AAM67631; BUsg_060.
DR   KEGG; bas:BUsg_060; -.
DR   eggNOG; COG2190; Bacteria.
DR   HOGENOM; CLU_012312_5_1_6; -.
DR   OMA; HTKHAVG; -.
DR   OrthoDB; 1481289at2; -.
DR   Proteomes; UP000000416; 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; Sugar transport; Transferase; Transport; Zinc.
FT   CHAIN           1..167
FT                   /note="PTS system glucose-specific EIIA component"
FT                   /id="PRO_0000186539"
FT   DOMAIN          37..141
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        89
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783,
FT                   ECO:0000255|PROSITE-ProRule:PRU00416"
FT   BINDING         74
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P69783, ECO:0000305"
FT   BINDING         89
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P69783, ECO:0000305"
FT   SITE            74
FT                   /note="Important for phospho-donor activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   MOD_RES         89
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
SQ   SEQUENCE   167 AA;  18329 MW;  9C71B05BC7907551 CRC64;
     MSFFSGFFNK KKSKYSKKID ILAPLSGDII NIEDVPDVVF SKKIVGDGIA INPTGNKILA
     PINGTIGKIL NSMHAFSIIS EEGVELFVHF GIDTVKLRGE GFKQIAQDNQ KVKIGDTIIL
     FDLNLLKEKA RSILTPVVIS NIEKFKNIEK SSGTIIAGKT IIMSLYN