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Database: UniProt
Entry: P75146
LinkDB: P75146
Original site: P75146 
ID   PTMCB_MYCPN             Reviewed;         488 AA.
AC   P75146;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 2.
DT   02-NOV-2016, entry version 110.
DE   RecName: Full=PTS system mannitol-specific EIICB component {ECO:0000250|UniProtKB:P28008};
DE   AltName: Full=EIICB-Mtl {ECO:0000250|UniProtKB:P28008};
DE            Short=EII-Mtl {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P28008};
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P28008};
DE              EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550, ECO:0000250|UniProtKB:P28008};
DE     AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P28008};
GN   Name=mtlA; OrderedLocusNames=MPN_651; ORFNames=MP191;
OS   Mycoplasma pneumoniae (strain ATCC 29342 / M129).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C.,
RA   Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar
CC       phosphotransferase system (sugar PTS), a major carbohydrate active
CC       transport system, catalyzes the phosphorylation of incoming sugar
CC       substrates concomitantly with their translocation across the cell
CC       membrane. The enzyme II CmtAB PTS system is involved in D-mannitol
CC       transport. {ECO:0000250|UniProtKB:P28008}.
CC   -!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + D-
CC       mannitol(Side 1) = [protein]-L-histidine + D-mannitol 1-
CC       phosphate(Side 2). {ECO:0000250|UniProtKB:P00550,
CC       ECO:0000250|UniProtKB:P28008}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P28008}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00427}; Multi-pass membrane protein
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The EIIC type-2 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- DOMAIN: The PTS EIIB type-2 domain is phosphorylated by phospho-
CC       EIIA on a cysteinyl residue. Then, it transfers the phosphoryl
CC       group to the sugar substrate concomitantly with the sugar uptake
CC       processed by the PTS EIIC type-2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00422}.
CC   -!- SIMILARITY: Contains 1 PTS EIIB type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC   -!- SIMILARITY: Contains 1 PTS EIIC type-2 domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00427}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB95839.1; Type=Frameshift; Positions=55, 68; Evidence={ECO:0000305};
DR   EMBL; U00089; AAB95839.1; ALT_FRAME; Genomic_DNA.
DR   PIR; S73517; S73517.
DR   RefSeq; NP_110340.1; NC_000912.1.
DR   ProteinModelPortal; P75146; -.
DR   EnsemblBacteria; AAB95839; AAB95839; MPN_651.
DR   GeneID; 877002; -.
DR   KEGG; mpn:MPN651; -.
DR   PATRIC; 20022785; VBIMycPne110_0715.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; MLVNNFY; -.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0022872; F:protein-N(PI)-phosphohistidine-mannitol phosphotransferase system transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   CDD; cd05567; PTS_IIB_mannitol; 1.
DR   Gene3D; 3.40.50.10370; -; 1.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR029503; PTS_EIIB_mannitol.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Complete proteome; Kinase; Membrane; Phosphoprotein;
KW   Phosphotransferase system; Reference proteome; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    488       PTS system mannitol-specific EIICB
FT                                component.
FT                                /FTId=PRO_0000186619.
FT   TOPO_DOM      1     26       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     27     48       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     49     52       Extracellular.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     53     73       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     74    147       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    148    169       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    170    178       Extracellular.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    179    199       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    200    289       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    290    309       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    310    331       Extracellular.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    332    353       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    354    488       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   DOMAIN       15    362       PTS EIIC type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   DOMAIN      397    488       PTS EIIB type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00422}.
FT   ACT_SITE    403    403       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008}.
FT   MOD_RES     403    403       Phosphocysteine; by EIIA.
FT                                {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008,
FT                                ECO:0000255|PROSITE-ProRule:PRU00422}.
SQ   SEQUENCE   488 AA;  53440 MW;  E4CDE1411110C9C4 CRC64;
     MRKKLAKVKV HIQSLDSLLS SMTMPIIGIF IAWGLLASFF IPSGWTPDKN LALMVGIGIQ
     YVIPTIIXFF GGKKIYEIRG GVIAVIIAIA VIAAGQTEAF TKIVGQKSVM FLGVMIFGPI
     AALILKHTEK FWIHRIKSGF EMLVNNFYLG FLGFALIFPS FYLSIYLIGY IQLGLKLLVE
     IMQQYKLYPI AAIVIEPAKV LFLNNAINHG VLTPLGLQQV RDSGKSILFL LESNPGPGLG
     LLVAFLIFFF KRDKKLSSNA ASSSPIHLFG GIHEVYFPFV LLKPVLILAT IAVGVVGNGI
     LQIFNAGTIA PVSPGSVIAG FLQINKTPLD VAGYALALVL SAVTSLLISL LLLSLTRKKQ
     LKTLQEAQAQ VAEMKQTPAK KPRQKDTPAI ATKIDFSQVT FVCDAGMGSS TMGAAIFRKE
     LKNQNIEDIT VINKAIVDLK DEKVIITISQ LYDRVKAKRA DATIYTINQF LDKQGYLTII
     EKIKNEKN
//
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