PTMA_STAAW
ID PTMA_STAAW Reviewed; 144 AA.
AC P0A0D9; P17875; Q9RL67;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=EIIA {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=EIII {ECO:0000250|UniProtKB:P0A0E0};
DE AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P0A0E0};
GN Name=mtlF; Synonyms=mtlA; OrderedLocusNames=MW2084;
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 CmtAB PTS system is involved in D-mannitol transport.
CC {ECO:0000250|UniProtKB:P0A0E0}.
CC -!- SUBUNIT: Homodimer or homotrimer. Seems to be a monomer when not
CC phosphorylated. {ECO:0000250|UniProtKB:P0A0E0}.
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 EMBL; BA000033; BAB95949.1; -; Genomic_DNA.
DR RefSeq; WP_001292149.1; NC_003923.1.
DR AlphaFoldDB; P0A0D9; -.
DR SMR; P0A0D9; -.
DR EnsemblBacteria; BAB95949; BAB95949; BAB95949.
DR GeneID; 66840368; -.
DR KEGG; sam:MW2084; -.
DR HOGENOM; CLU_072531_3_0_9; -.
DR OMA; EDYIQAM; -.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
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.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transferase; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..144
FT /note="Mannitol-specific phosphotransferase enzyme IIA
FT component"
FT /id="PRO_0000186641"
FT DOMAIN 3..142
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 63
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0A0E0,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT MOD_RES 63
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P0A0E0"
SQ SEQUENCE 144 AA; 15542 MW; B166851EEBC3A5AA CRC64;
MSELFSNDNI FLNVNVNSQN EAIEKAGKAL VDSGAVTDAY IQAMKDREQV VSTFMGNGLA
IPHGTDEAKT NVIHSGLTLL QIPEGVDWDG EVVKVVVGIA GKDGEHLDLL SKIAITFSEE
ENVDRIVQAK SAEEIKQVFE EADA
