PTMCB_MYCPN
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 03-AUG-2022, entry version 126.
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) (Mycoplasmoides
OS pneumoniae).
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., 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 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:P28008}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-mannitol(out) + N(pros)-phospho-L-histidyl-[protein] = D-
CC mannitol 1-phosphate(in) + L-histidyl-[protein];
CC Xref=Rhea:RHEA:33363, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746,
CC ChEBI:CHEBI:16899, ChEBI:CHEBI:29979, ChEBI:CHEBI:61381,
CC ChEBI:CHEBI:64837; EC=2.7.1.197;
CC Evidence={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 {ECO:0000255|PROSITE-
CC 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-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00422}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB95839.1; Type=Frameshift; 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 STRING; 272634.MPN_651; -.
DR EnsemblBacteria; AAB95839; AAB95839; MPN_651.
DR KEGG; mpn:MPN_651; -.
DR PATRIC; fig|272634.6.peg.715; -.
DR HOGENOM; CLU_028721_2_0_14; -.
DR OMA; GWAIKRF; -.
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 GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05567; PTS_IIB_mannitol; 1.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
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; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..488
FT /note="PTS system mannitol-specific EIICB component"
FT /id="PRO_0000186619"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 27..48
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 49..52
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 53..73
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 74..147
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 148..169
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 170..178
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 200..289
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 290..309
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 310..331
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 332..353
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 354..488
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT DOMAIN 15..362
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 397..488
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT ACT_SITE 403
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008"
FT MOD_RES 403
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008, ECO:0000255|PROSITE-
FT 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
