PTMCB_STACA
ID PTMCB_STACA Reviewed; 518 AA.
AC P28008;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 25-MAY-2022, entry version 115.
DE RecName: Full=PTS system mannitol-specific EIICB component {ECO:0000303|PubMed:1551396};
DE AltName: Full=EIICB-Mtl {ECO:0000303|PubMed:1551396};
DE Short=EII-Mtl {ECO:0000303|PubMed:1551396};
DE Includes:
DE RecName: Full=Mannitol permease IIC component {ECO:0000303|PubMed:1551396};
DE AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000303|PubMed:1551396};
DE Includes:
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:1551396};
DE EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550};
DE AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000303|PubMed:1551396};
GN Name=mtlA {ECO:0000303|PubMed:1551396};
OS Staphylococcus carnosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1281;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=1551396; DOI=10.1111/j.1432-1033.1992.tb16717.x;
RA Fischer R., Hengstenberg W.;
RT "Mannitol-specific enzyme II of the phosphoenolpyruvate-dependent
RT phosphotransferase system of Staphylococcus carnosus. Sequence and
RT expression in Escherichia coli and structural comparison with the enzyme
RT IImannitol of Escherichia coli.";
RL Eur. J. Biochem. 204:963-969(1992).
RN [2]
RP SEQUENCE REVISION.
RA Hengstenberg W.;
RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 504-518, FUNCTION, SUBUNIT, ACTIVE SITE, AND
RP PHOSPHORYLATION AT CYS-432.
RX PubMed=7588734; DOI=10.1111/j.1432-1033.1995.116_1.x;
RA Pogge von Strandmann R., Weigt C., Fischer R., Meyer H.E., Kalbitzer H.R.,
RA Hengstenberg W.;
RT "Expression, purification and characterization of the enzyme II mannitol-
RT specific domain from Staphylococcus carnosus and determination of the
RT active-site cysteine residue.";
RL Eur. J. Biochem. 233:116-122(1995).
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:0000269|PubMed:1551396, ECO:0000305|PubMed:7588734}.
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, ECO:0000305|PubMed:1551396};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:7588734}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00427, ECO:0000305|PubMed:1551396}; Multi-pass membrane
CC protein {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-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; X56333; CAA39769.1; -; Genomic_DNA.
DR PIR; S68193; S22385.
DR AlphaFoldDB; P28008; -.
DR SMR; P28008; -.
DR iPTMnet; P28008; -.
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: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 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; 1.
DR TIGRFAMs; TIGR00851; mtlA; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Membrane; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..518
FT /note="PTS system mannitol-specific EIICB component"
FT /id="PRO_0000186626"
FT TOPO_DOM 1..31
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 54..57
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 79..142
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 143..164
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 165..173
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 195..281
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 282..301
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 302..321
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 322..343
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TOPO_DOM 344..518
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT DOMAIN 20..352
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 426..518
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT REGION 369..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 432
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000305|PubMed:7588734"
FT MOD_RES 432
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422,
FT ECO:0000269|PubMed:7588734"
SQ SEQUENCE 518 AA; 55686 MW; A0DE0B9E4BA74FA5 CRC64;
MDTMSNSQQN KGIGRKVQAF GSFLSSMIMP NIGAFIAWGF IAAIFIDNGW FPNKDLAQLA
GPMITYLIPL LIAFSGGRLI HDLRGGIIAA TATMGVIVAL PDTPMLLGAM IMGPLVGWLM
KKTDEFVQPR TPQGFEMLFN NFSAGILGFI MTIFGFEVLA PIMKFIMHIL SVGVEALVHA
HLLPLVSILV EPAKIVFLNN AINHGVFTPL GADQAAHAGQ SILYTIESNP GPGIGVLIAY
MIFGKGTAKA TSYGAGIIQF FGGIHEIYFP YVLMRPLLFV SVILGGMTGV ATYSLLDFGF
KTPASPGSII VYAINAPKGE FLHMLTGVVL AALVSFVVSA LILKFTKDPK QDLAEATAQM
EATKGKKSSV ASKLSAKDDN KAADNKTAET TTATAASNKA EDKDSDELLD DYNTEDVDAH
NYNNVDHVIF ACDAGMGSSA MGASMLRNKF KNAGLENIQV TNTAINQLPK NAQLVITQKK
LTDRAIKQSP DAIHISVENF LNSPRYEELI NNLKEDQD
