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Database: UniProt
Entry: P69827
LinkDB: P69827
Original site: P69827 
ID   PTMCB_ECO57             Reviewed;         462 AA.
AC   P69827; P32059;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   02-NOV-2016, entry version 77.
DE   RecName: Full=PTS system mannitol-specific cryptic EIICB component {ECO:0000250|UniProtKB:P69826};
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=cmtA; OrderedLocusNames=Z4277, ECs3808;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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   -!- SUBCELLULAR LOCATION: Cell inner 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}.
DR   EMBL; AE005174; AAG58063.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB37231.1; -; Genomic_DNA.
DR   PIR; H91104; H91104.
DR   RefSeq; NP_311835.1; NC_002695.1.
DR   RefSeq; WP_000428805.1; NZ_LPWC02000002.1.
DR   ProteinModelPortal; P69827; -.
DR   SMR; P69827; -.
DR   STRING; 155864.Z4277; -.
DR   EnsemblBacteria; AAG58063; AAG58063; Z4277.
DR   EnsemblBacteria; BAB37231; BAB37231; BAB37231.
DR   GeneID; 916373; -.
DR   KEGG; ece:Z4277; -.
DR   KEGG; ecs:ECs3808; -.
DR   PATRIC; 18357107; VBIEscCol44059_3732.
DR   eggNOG; ENOG4105CTS; Bacteria.
DR   eggNOG; COG2213; LUCA.
DR   HOGENOM; HOG000252814; -.
DR   KO; K02799; -.
DR   KO; K02800; -.
DR   OMA; DIVVTHE; -.
DR   BioCyc; ECOO157:CMTA-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; IPR003352; PTS_EIIC.
DR   InterPro; IPR013014; PTS_EIIC_2.
DR   InterPro; IPR004718; PTS_IIC_mtl.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   TIGRFAMs; TIGR00851; mtlA; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR   PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Complete proteome; Kinase;
KW   Membrane; Phosphoprotein; Phosphotransferase system; Sugar transport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN         1    462       PTS system mannitol-specific cryptic
FT                                EIICB component.
FT                                /FTId=PRO_0000186680.
FT   TOPO_DOM      1     24       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     25     46       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     47     50       Periplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM     51     71       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM     72    134       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    135    156       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    157    165       Periplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    166    186       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    187    273       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    274    293       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    294    313       Periplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   TRANSMEM    314    335       Helical. {ECO:0000250|UniProtKB:P00550}.
FT   TOPO_DOM    336    462       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P00550}.
FT   DOMAIN       13    344       PTS EIIC type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00427}.
FT   DOMAIN      371    461       PTS EIIB type-2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00422}.
FT   ACT_SITE    377    377       Phosphocysteine intermediate; for EIIB
FT                                activity. {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008}.
FT   MOD_RES     377    377       Phosphocysteine; by EIIA.
FT                                {ECO:0000250|UniProtKB:P00550,
FT                                ECO:0000250|UniProtKB:P28008,
FT                                ECO:0000255|PROSITE-ProRule:PRU00422}.
SQ   SEQUENCE   462 AA;  48971 MW;  83F2D203D9E5A4C4 CRC64;
     MENKSARAKV QAFGGFLTAM VIPNIGAFIA WGFITALFIP TGWLPNEHFA KIVGPMITYL
     LPVMIGSTGG HLVGGKRGAV MGGIGTIGVI VGAEIPMFLG SMIMGPLGGL VIKYVDKALE
     KRIPAGFEMV INNFSLGIAG MLLCLLGFEV IGPAVLIANT FVKECIEALV HAGYLPLLSV
     INEPAKVLFL NNAIDQGVYY PLGMQQASVN GKSIFFMVAS NPGPGLGLLL AFTLFGKGMS
     KRSAPGAMII HFLGGIHELY FPYVLMKPLT IIAMIAGGMS GTWMFNLLDG GLVAGPSPGS
     IFAYLALTPK GSFLATIAGV TVGTLVSFAI TSLILKMEKT VETESEDEFA QSANAVKAMK
     QEGAFSLSRV KRIAFVCDAG MGSSAMGATT FRKRLEKAGL AIEVKHYAIE NVPADADIVV
     THASLEGRVK RVTDKPLILI NNYIGDPKLD TLFNQLTAEH KH
//
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