PTMCB_STRPN
ID PTMCB_STRPN Reviewed; 589 AA.
AC Q97SH4;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=SP_0394;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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}.
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DR EMBL; AE005672; AAK74558.1; -; Genomic_DNA.
DR PIR; E95045; E95045.
DR RefSeq; WP_000391672.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97SH4; -.
DR SMR; Q97SH4; -.
DR STRING; 170187.SP_0394; -.
DR EnsemblBacteria; AAK74558; AAK74558; SP_0394.
DR KEGG; spn:SP_0394; -.
DR eggNOG; COG2213; Bacteria.
DR OMA; GWAIKRF; -.
DR PhylomeDB; Q97SH4; -.
DR BioCyc; SPNE170187:G1FZB-410-MON; -.
DR Proteomes; UP000000585; 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; 2.
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; 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; 2.
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 membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..589
FT /note="PTS system mannitol-specific EIICB component"
FT /id="PRO_0000186630"
FT TOPO_DOM 1..25
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 26..47
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 48..51
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 73..135
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 158..166
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 188..274
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 275..294
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 295..316
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 317..338
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 339..589
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT DOMAIN 14..347
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 381..476
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT ACT_SITE 387
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008"
FT MOD_RES 387
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000250|UniProtKB:P28008, ECO:0000255|PROSITE-
FT ProRule:PRU00422"
SQ SEQUENCE 589 AA; 61855 MW; A7F565D63682DC97 CRC64;
MEEKVSLKVR VQKLGTSLSN MVMPNIGAFI AWGVLTALFI ADGYLPNEQL ATVVGPMLTY
LLPILIGYTG GYMIHGQRGA VVGAIATVGA ITGSSVPMFI GAMVMGPLGG WTIKKFDEKF
QEKIRPGFEM LVNNFSAGLV GFALLLLAFY AIGPVVSTLT GAVGNGVEAI VNARLLPMAN
IIIEPAKVLF LNNALNHGIF TPLGVEQVAQ AGKSILFLLE ANPGPGLGIL LAYAVFGKGS
AKSSSWGAMV IHFFGGIHEI YFPYVMMKPT LFLAAMAGGI SGTFTFQLLD AGLKSPASPG
SIIAIIATAP KGVWPHLNVL LGVLVAAVVS FLVAALILHA DKSTEDSLEA AQAATQAAKA
QSKGQLVSTS VDAVVSTDSV EKIIFACDAG MGSSAMGASI LRDKVKKAGL EIPVSNQAIS
NLLDTPKTLI VTQEELTPRA KDKSPSAIHV SVDNFLASSR YDEIVASLTG ASPIAEIEGD
IPTSAPVDSQ ESDLNHIDAV VVAYGKAQGT ATMGCETIRA IFRNKNIRIP VSTAKISELG
EFNSKNIMIV TTISLQAEVQ QAAPNSQFLI VDSLVTTPEY DKMAARMYK
