PTM3C_BUCAP
ID PTM3C_BUCAP Reviewed; 649 AA.
AC Q8K911;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=BUsg_552;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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-563 and
CC Cys-386. {ECO:0000250|UniProtKB:P00550}.
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DR EMBL; AE013218; AAM68090.1; -; Genomic_DNA.
DR RefSeq; WP_011054056.1; NC_004061.1.
DR AlphaFoldDB; Q8K911; -.
DR SMR; Q8K911; -.
DR STRING; 198804.BUsg_552; -.
DR PRIDE; Q8K911; -.
DR EnsemblBacteria; AAM68090; AAM68090; BUsg_552.
DR KEGG; bas:BUsg_552; -.
DR eggNOG; COG2213; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_028721_1_0_6; -.
DR OMA; GWAIKRF; -.
DR OrthoDB; 554815at2; -.
DR Proteomes; UP000000416; 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 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 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..649
FT /note="PTS system mannitol-specific EIICBA component"
FT /id="PRO_0000186612"
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..340
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 380..472
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 503..645
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 386
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT ACT_SITE 563
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT SITE 547
FT /note="Stabilizes the transition state in the phosphoryl
FT transfer from HPr to EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT MOD_RES 386
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00422"
FT MOD_RES 563
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550"
SQ SEQUENCE 649 AA; 72358 MW; B365CE4719C986C0 CRC64;
MFRLITLKIQ NFGQFLSNMI MPNISIFITW GIMNSLFLSL DWQYNKIFAQ LISPIIFYLL
PILIGYTGGS LIAGQRGGLL GSITTIGMIT STDMPMFLGG MVAGPLGGWI IKGFDQIIKN
RIKSGFEMLV NNFSIAIIGI FLTIFSFFFI GPFIEGVSKF LGCLIKIIID FNLLPLIAFI
IEPAKVFFLN NAINHGIFSP LGIQEISENK SSLFFLIESN PGPGLGILIA CFFFGKEKSY
KSSGTAAIVQ FLGGIHEIYF SYVLIKPILM ISLILGSMTS IFMLVFFKGG LIAAVSPGSI
LSILAMTKKG LYFANLISIF SSFLISFLSA MLFFKINLGQ KIKNDKSSIQ LFKNNLFPIK
KIGDEKYDFI KKIKNFQKIK NIIIACDAGM GSSAMGASIL RKKIKSNNLT HIYVSNIAIN
LLPKNADLVI THEKLTYLAK KRAPDAQHIS LTNFLDSNFY TSLVKQLDLN KDFFKKNNIQ
DKKDRITQIN IDSHKEIQSK CFFQISDKNI FLNQYAENKK EAIKIVGKHL VAQGYVKKDY
IDAMLDREKI ASTWLGESVA LPHGTIKSKD SILKTGVIFC QFPKGVHFGE TIDDIAYLVI
GIAAKNNEHI MVVSNITNAL DDKDVISKLS KTKSVKEVLS YLNVNVKKN
