ID   PTGA_BUCBP              Reviewed;         168 AA.
AC   Q89B05;
DT   30-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2003, 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=bbp_059;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(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   -!- 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE016826; AAO26798.1; -; Genomic_DNA.
DR   RefSeq; WP_011091199.1; NC_004545.1.
DR   AlphaFoldDB; Q89B05; -.
DR   SMR; Q89B05; -.
DR   STRING; 224915.bbp_059; -.
DR   EnsemblBacteria; AAO26798; AAO26798; bbp_059.
DR   GeneID; 56470603; -.
DR   KEGG; bab:bbp_059; -.
DR   eggNOG; COG2190; Bacteria.
DR   HOGENOM; CLU_012312_5_1_6; -.
DR   OMA; HTKHAVG; -.
DR   OrthoDB; 1481289at2; -.
DR   Proteomes; UP000000601; 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.
PE   3: Inferred from homology;
KW   Cytoplasm; Kinase; Metal-binding; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transport; Zinc.
FT   CHAIN           1..168
FT                   /note="PTS system glucose-specific EIIA component"
FT                   /id="PRO_0000186540"
FT   DOMAIN          38..142
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        90
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783,
FT                   ECO:0000255|PROSITE-ProRule:PRU00416"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P69783, ECO:0000305"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P69783, ECO:0000305"
FT   SITE            75
FT                   /note="Important for phospho-donor activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   MOD_RES         90
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
SQ   SEQUENCE   168 AA;  18507 MW;  3F49BABA46C9BB00 CRC64;
     MKFFSNFFKN KNNLSSHNVI NIFAPISGDI VEIESVPDEV FSNKIVGDGI AISPNSNILL
     APINGTIGRI FETLHAFSIK SDDDIELFVH FGIDTVKLKG RGFKKISEEN IAVKIGDPII
     FIDLPFLKKL VKSTLTPVII SNIDKFKKIT KNTGSVIAGK TVIFSVQK