PTM3C_PASMU
ID PTM3C_PASMU Reviewed; 624 AA.
AC Q9CLY8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
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=PM1061;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(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. 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-542 and
CC Cys-378. {ECO:0000250|UniProtKB:P00550}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK03145.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE004439; AAK03145.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_005754557.1; NC_002663.1.
DR AlphaFoldDB; Q9CLY8; -.
DR SMR; Q9CLY8; -.
DR STRING; 747.DR93_904; -.
DR PRIDE; Q9CLY8; -.
DR EnsemblBacteria; AAK03145; AAK03145; PM1061.
DR KEGG; pmu:PM1061; -.
DR PATRIC; fig|272843.6.peg.1075; -.
DR HOGENOM; CLU_028721_1_0_6; -.
DR OMA; GWAIKRF; -.
DR Proteomes; UP000000809; 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; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05567; PTS_IIB_mannitol; 1.
DR Gene3D; 3.40.930.10; -; 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 Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR SUPFAM; SSF55804; SSF55804; 1.
DR TIGRFAMs; TIGR00851; mtlA; 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..624
FT /note="PTS system mannitol-specific EIICBA component"
FT /id="PRO_0000186616"
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..336
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 372..463
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 482..624
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 378
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT ACT_SITE 542
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT SITE 526
FT /note="Stabilizes the transition state in the phosphoryl
FT transfer from HPr to EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT MOD_RES 378
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00422"
FT MOD_RES 542
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550"
SQ SEQUENCE 624 AA; 66550 MW; EA104312CEE2D891 CRC64;
MLSANAKVKV QNFGRFLSNM VMPNIGAFIA WGFITALFIP TGWLPNETLA KLVGPMITYL
LPLLIGYSGG KLIAGERGAV VGAIATAGVI VGTDIPMFLG AMIAGPTGGW AIKRFDKWAD
GKIKSGFEML VNNFSSGIIG MILAILFFWL IGPAVKALST MLAAGVDILV KAHLLPLTSI
FVEPAKILFL NNAINHGIFS PLGIQQSQEF GQSIFFLIEA NPGPGLGVLL AYIIFGKGTA
KQTAGGATII HFFGGIHEIY FPYVLMNPRL LLAVIAGGVS GVFTLVLFNA GLVAPASPGS
IIAVLLMTPQ NAIVGVLASV AIAATVSFVI ASFFLKIQKE ENGHSLEKMQ AASKAMKSGV
QFNTPARYQG VQKIFVACDA GMGSSAMGAS MLRKKVKEAG LAIEVTNCAI NDLPEDAQLV
ITHQDLTLRA KKHTPNAMHF SLNNFLDAHF YDNLVQDLSN TKVADLAKVS TLEPQEAPQT
AFVLTEKQVF LGLKAANKEE AIRFAGERLV ESGFVLPSYV DAMFEREKMV STYLGEGIAV
PHGTIEAKDA VLKTGVVVCQ YPEGVKFNED EEDSIAKLVI GIAAKNNEHL QVVSAITNAL
DNEDAIRILS ETDDVEKVLA LLKA
