ID PTM3C_VIBCH Reviewed; 649 AA.
AC Q9KKQ7;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 151.
DE RecName: Full=PTS system mannitol-specific EIICBA component {ECO:0000250|UniProtKB:P00550};
DE AltName: Full=EIICBA-Mtl {ECO:0000250|UniProtKB:P00550};
DE Short=EII-Mtl {ECO:0000250|UniProtKB:P00550};
DE Includes:
DE RecName: Full=Mannitol permease IIC component {ECO:0000250|UniProtKB:P00550};
DE AltName: Full=PTS system mannitol-specific EIIC component {ECO:0000250|UniProtKB:P00550};
DE Includes:
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P00550};
DE EC=2.7.1.197 {ECO:0000250|UniProtKB:P00550};
DE AltName: Full=PTS system mannitol-specific EIIB component {ECO:0000250|UniProtKB:P00550};
DE Includes:
DE RecName: Full=Mannitol-specific phosphotransferase enzyme IIA component {ECO:0000250|UniProtKB:P00550};
DE AltName: Full=PTS system mannitol-specific EIIA component {ECO:0000250|UniProtKB:P00550};
GN Name=mtlA; OrderedLocusNames=VC_A1045;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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. This
CC system is involved in D-mannitol transport.
CC {ECO:0000250|UniProtKB:P00550}.
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 -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00550}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P00550, ECO:0000255|PROSITE-ProRule:PRU00427};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P00550,
CC ECO:0000255|PROSITE-ProRule:PRU00427}.
CC -!- INDUCTION: Induced by mannitol. Repressed by MltR.
CC {ECO:0000250|UniProtKB:P00550}.
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 -!- DOMAIN: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on
CC a histidyl residue. Then, it transfers the phosphoryl group to the PTS
CC EIIB type-2 domain. {ECO:0000255|PROSITE-ProRule:PRU00417}.
CC -!- PTM: An intramolecular phosphotransfer takes places between His-564 and
CC Cys-390. {ECO:0000250|UniProtKB:P00550}.
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DR EMBL; AE003853; AAF96939.1; -; Genomic_DNA.
DR PIR; B82385; B82385.
DR RefSeq; NP_233427.1; NC_002506.1.
DR RefSeq; WP_000625706.1; NZ_LT906615.1.
DR AlphaFoldDB; Q9KKQ7; -.
DR SMR; Q9KKQ7; -.
DR STRING; 243277.VC_A1045; -.
DR TCDB; 4.A.2.1.12; the pts fructose-mannitol (fru) family.
DR DNASU; 2612120; -.
DR EnsemblBacteria; AAF96939; AAF96939; VC_A1045.
DR KEGG; vch:VC_A1045; -.
DR PATRIC; fig|243277.26.peg.3651; -.
DR eggNOG; COG2213; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_028721_1_0_6; -.
DR Proteomes; UP000000584; Chromosome 2.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05567; PTS_IIB_mannitol; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR016152; PTrfase/Anion_transptr.
DR InterPro; IPR002178; PTS_EIIA_type-2_dom.
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 NCBIfam; TIGR00851; mtlA; 1.
DR PANTHER; PTHR30181; MANNITOL PERMEASE IIC COMPONENT; 1.
DR PANTHER; PTHR30181:SF2; PTS SYSTEM MANNITOL-SPECIFIC EIICBA COMPONENT; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR PROSITE; PS00372; PTS_EIIA_TYPE_2_HIS; 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; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..649
FT /note="PTS system mannitol-specific EIICBA component"
FT /id="PRO_0000186617"
FT TRANSMEM 25..46
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 135..156
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 166..186
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 274..293
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT TRANSMEM 314..335
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT DOMAIN 13..342
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 384..475
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 504..646
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 390
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT ACT_SITE 564
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT SITE 548
FT /note="Stabilizes the transition state in the phosphoryl
FT transfer from HPr to EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT MOD_RES 390
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00422"
FT MOD_RES 564
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550"
SQ SEQUENCE 649 AA; 68674 MW; D2C67C27D8BE99CA CRC64;
MISSDAKVKI QNFGRFLSNM VMPNIGAFIA WGFITALFIP TGWVPNETLA SLVGPMITYL
LPLLIGYTGG KLAGGERGAV VGAITTMGVI VGTDIPMFMG AMIVGPMGGW AIKAFDKKID
GKVRSGFEML VNNFSAGIIG MLCAIIAFFL IGPFVKVLSG ALAAGVNFLV TAHLLPLTSI
FVEPAKILFL NNAINHGIFS PLGIQQASET GQSIFFLIEA NPGPGLGILL AYMVFGKGTA
RQTAGGATII HFFGGIHEIY FPYILMNPRL ILAAIAGGMT GVFTLTVFNA GLVSPASPGS
IFAVLLMTNK GSILGVVCSI FAAAAVSFTV AALLMKAQTS TEQDGDKDAL VKATSIMQEM
KAGSKGQAAP TATQSKKIDM ANVQSIIVAC DAGMGSSAMG ASMLRKKIQE VGLPVTVTNM
AINSLPAHVD MVITHQDLTD RARQHAPNAE HISLNNFLDS ALYNQLVTQL LAAKRQAAND
SQLIKPSILA ANDDRYEVQQ PSVFQLQKEN IHLGLNAKNK EEAIRFAGNK LVELGYVHPE
YVDAMFEREK LVSTYLGESI AVPHGTVDAK DRVIKTGIVI CQYPQGVAFS EDSGDVAKLV
IGIAAKNDEH IQVITTITNA LDDPNAIDKL TSTKDVSDVL SILATSQAA
//
