ID   PTGA_STAAW              Reviewed;         166 AA.
AC   Q8NWR1;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=MW1312;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(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       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; BA000033; BAB95177.1; -; Genomic_DNA.
DR   RefSeq; WP_000473657.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWR1; -.
DR   SMR; Q8NWR1; -.
DR   EnsemblBacteria; BAB95177; BAB95177; BAB95177.
DR   KEGG; sam:MW1312; -.
DR   HOGENOM; CLU_012312_5_3_9; -.
DR   OMA; HTKHAVG; -.
DR   Proteomes; UP000000418; 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..166
FT                   /note="PTS system glucose-specific EIIA component"
FT                   /id="PRO_0000186553"
FT   DOMAIN          34..138
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   ACT_SITE        86
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783,
FT                   ECO:0000255|PROSITE-ProRule:PRU00416"
FT   BINDING         71
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         86
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            71
FT                   /note="Important for phospho-donor activity"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
FT   MOD_RES         86
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P69783"
SQ   SEQUENCE   166 AA;  17991 MW;  BD5299B744219982 CRC64;
     MFKKLFGKGK EVQKDIAIYT PLTGEFVKIE DIPDPVFAQK MMGEGFGINP TEGEVVSPIA
     GRVDNVFPTK HAIGLKADNG LELLVHIGLD TVQLDGEGFE VLVSSGDEVN VGDPLVRFNL
     EYINNNAKSV ISPIIITNTD QAASINIYDE NAVIKGETKV IDVTMN