PTMA_STACT
ID PTMA_STACT Reviewed; 144 AA.
AC P17876; B9DM95;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 132.
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};
GN Name=mtlF {ECO:0000303|PubMed:3064811}; OrderedLocusNames=Sca_1660;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2684783; DOI=10.1016/0378-1119(89)90050-4;
RA Fisher R., Eisermann R., Reiche B., Hengstenberg W.;
RT "Cloning, sequencing and overexpression of the mannitol-specific enzyme-
RT III-encoding gene of Staphylococcus carnosus.";
RL Gene 82:249-257(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
RN [3]
RP PROTEIN SEQUENCE OF 2-18 AND 49-66, FUNCTION, ACTIVE SITE, PHOSPHORYLATION
RP AT HIS-63, AND SUBUNIT.
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 EMBL; M30781; AAA26656.1; -; Genomic_DNA.
DR EMBL; AM295250; CAL28566.1; -; Genomic_DNA.
DR PIR; B31048; B31048.
DR PIR; JQ0088; JQ0088.
DR RefSeq; WP_015900906.1; NC_012121.1.
DR AlphaFoldDB; P17876; -.
DR SMR; P17876; -.
DR STRING; 396513.SCA_1660; -.
DR iPTMnet; P17876; -.
DR GeneID; 60544629; -.
DR KEGG; sca:SCA_1660; -.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_072531_3_0_9; -.
DR OMA; EDYIQAM; -.
DR OrthoDB; 1810962at2; -.
DR BioCyc; SCAR396513:SCA_RS08420-MON; -.
DR Proteomes; UP000000444; 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 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..144
FT /note="Mannitol-specific phosphotransferase enzyme IIA
FT component"
FT /id="PRO_0000186643"
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:0000255|PROSITE-ProRule:PRU00417,
FT ECO:0000305|PubMed:3064811"
FT MOD_RES 63
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000305|PubMed:3064811"
SQ SEQUENCE 144 AA; 15566 MW; 77ACE463AFF17957 CRC64;
MTELFSNENI FLNQSFEDQN EAIEKAGQAL VDAGAVTEDY IQAMKDREAV VSTFMGNGLA
IPHGTDEAKS AVLQSGLTLL QIPEGVQWGD DVAKVVVGIA GKDGEHLDLL SKIAITFSEE
ENVDRIVNTK SPEEIKAVFE EADV
