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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   01-OCT-2014, entry version 101.
DE   RecName: Full=PTS system mannitol-specific EIICB component;
DE   AltName: Full=EIICB-Mtl;
DE            Short=EII-Mtl;
DE   Includes:
DE     RecName: Full=Mannitol permease IIC component;
DE     AltName: Full=PTS system mannitol-specific EIIC component;
DE   Includes:
DE     RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.69;
DE     AltName: Full=PTS system mannitol-specific EIIB component;
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. This system is involved in mannitol transport (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY: Protein EIIB N(pi)-phospho-L-
CC       histidine/cysteine + sugar = protein EIIB + sugar phosphate.
CC       {ECO:0000255|PROSITE-ProRule:PRU00422}.
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 domain forms the PTS system translocation channel
CC       and contains the specific substrate-binding site.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
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};
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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   STRING; 272634.MPN651; -.
DR   EnsemblBacteria; AAB95839; AAB95839; MPN_651.
DR   GeneID; 877002; -.
DR   KEGG; mpn:MPN651; -.
DR   PATRIC; 20022785; VBIMycPne110_0715.
DR   eggNOG; COG2213; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; HEVHYAY; -.
DR   OrthoDB; EOG6FBWWQ; -.
DR   BioCyc; MPNE272634:GJ6Z-697-MONOMER; -.
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   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;
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   TRANSMEM     22     42       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM     51     71       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM     80    100       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    103    123       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    151    171       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    187    207       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    227    247       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    277    297       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    299    319       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   TRANSMEM    335    355       Helical. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
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}.
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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