ID   PTM3C_KLEPN             Reviewed;         635 AA.
AC   Q9XBM7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=PTS system mannitol-specific EIICBA component {ECO:0000303|PubMed:11164312};
DE   AltName: Full=EIICBA-Mtl {ECO:0000303|PubMed:11164312};
DE            Short=EII-Mtl {ECO:0000303|PubMed:11164312};
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 {ECO:0000303|PubMed:11164312};
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=11164312; DOI=10.1111/j.1574-6968.2001.tb09473.x;
RA   Otte S., Lengeler J.W.;
RT   "The mtl genes and the mannitol-1-phosphate dehydrogenase from Klebsiella
RT   pneumoniae KAY2026.";
RL   FEMS Microbiol. Lett. 194:221-227(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-554 and
CC       Cys-384. {ECO:0000250|UniProtKB:P00550}.
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DR   EMBL; AF166095; AAD45385.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XBM7; -.
DR   SMR; Q9XBM7; -.
DR   PRIDE; Q9XBM7; -.
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; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..635
FT                   /note="PTS system mannitol-specific EIICBA component"
FT                   /id="PRO_0000186615"
FT   TRANSMEM        24..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        134..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        165..185
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        273..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   TRANSMEM        313..334
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   DOMAIN          12..342
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT   DOMAIN          378..473
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT   DOMAIN          494..635
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT   ACT_SITE        384
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   ACT_SITE        554
FT                   /note="Tele-phosphohistidine intermediate; for EIIA
FT                   activity"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000255|PROSITE-ProRule:PRU00417"
FT   SITE            538
FT                   /note="Stabilizes the transition state in the phosphoryl
FT                   transfer from HPr to EIIA"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
FT   MOD_RES         384
FT                   /note="Phosphocysteine; by EIIA"
FT                   /evidence="ECO:0000250|UniProtKB:P00550,
FT                   ECO:0000255|PROSITE-ProRule:PRU00422"
FT   MOD_RES         554
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250|UniProtKB:P00550"
SQ   SEQUENCE   635 AA;  67698 MW;  9C76B771A03815E7 CRC64;
     MSSDIKIKVQ SFGRFLSNMV MPNIGAFIAW GIITALFIPT GWLPNETLAK LVGPMITYLL
     PLLIGYTGGK LVGGERGGVV GAITTMGVIV GADMPMFLGS MIAGPLGGYC IKKFDNWVDG
     KIKSGFEMLV NNFSAGIIGM ILAILAFLGI GPAVEVLSKI LAAGVNFMVA HDMLPLASIF
     VEPAKILFLN NAINHGIFSP LGIQQSHELG KSIFFLIEAN PGPGMGVLLA YMFFGRGSAK
     QSAGGAAIIH FLGGIHEIYF PYVLMNPRLI LAVILGGMTG VFTLTILNGG LVSPASPGSI
     LAVLAMTPKG AYFANIAAII AAMAVSFVVS AVLFKTSKVK ERSDIEAATR RMHDMKAESK
     GASPLAAGNV TNDLSHVRKI IVACDAGMGS SAMGAGVLRK KVQDAGLSNI SVTNSAINNL
     PPDVDLVITH RDLTERAMRQ VPQAQHISLT NFLDSGLYTS LTERLVAAQR HIDNEVKVTD
     SLKDSFDDTN NNLFQLGADN IFLGRKAATK EEANSFAGEQ LVKGGYVEPE YVQAMLDREK
     LTSTYLGESI AVPHGTIEAK DRVLKTGVVF CQYPEGVRFG EEEDEVARLV IGIAARNNEH
     IQVITSLTNA LDDETVIERL AKTTSVDEVL ALLNK