PTMA_STAAU
ID PTMA_STAAU Reviewed; 60 AA.
AC P0A0E0; P17875; Q9RL67;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 57.
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:3064811};
DE AltName: Full=EIIA {ECO:0000303|PubMed:3064811};
DE AltName: Full=EIII {ECO:0000303|PubMed:3064811};
DE AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000303|PubMed:3064811};
DE Flags: Fragments;
GN Name=mtlF {ECO:0000303|PubMed:3064811}; Synonyms=mtlA;
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP PROTEIN SEQUENCE OF 2-60, FUNCTION, ACTIVE SITE, PHOSPHORYLATION AT HIS-56,
RP AND SUBUNIT.
RC STRAIN=5601;
RX PubMed=3064811; DOI=10.1021/bi00417a047;
RA Reiche B., Frank R., Deutscher J., Meyer N., Hengstenberg W.;
RT "Staphylococcal phosphoenolpyruvate-dependent phosphotransferase system:
RT purification and characterization of the mannitol-specific enzyme IIImtl of
RT Staphylococcus aureus and Staphylococcus carnosus and homology with the
RT enzyme IImtl of Escherichia coli.";
RL Biochemistry 27:6512-6516(1988).
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 CmtAB PTS system is involved in D-mannitol transport.
CC {ECO:0000269|PubMed:3064811}.
CC -!- SUBUNIT: Homodimer or homotrimer. Seems to be a monomer when not
CC phosphorylated. {ECO:0000305|PubMed:3064811}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
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DR PIR; A31048; A31048.
DR AlphaFoldDB; P0A0E0; -.
DR SMR; P0A0E0; -.
DR iPTMnet; P0A0E0; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016301; F:kinase activity; 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; 3.40.930.10; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Direct protein sequencing; Kinase; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3064811"
FT CHAIN 2..>60
FT /note="Mannitol-specific phosphotransferase enzyme IIA
FT component"
FT /id="PRO_0000186642"
FT DOMAIN 2..>60
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 56
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000305|PubMed:3064811"
FT MOD_RES 56
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000305|PubMed:3064811"
FT NON_CONS 42..43
FT /evidence="ECO:0000305"
FT NON_TER 60
SQ SEQUENCE 60 AA; 6344 MW; EE0F554DF94ED20E CRC64;
MSELFSNDNI FLNVNVNSQN EAIEKAGKAL VDSGAVTDAY IQVVSTFMGN GLAIPHGTDD
