PTM3C_BUCBP
ID PTM3C_BUCBP Reviewed; 640 AA.
AC Q89A36;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=bbp_517;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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-556 and
CC Cys-385. {ECO:0000250|UniProtKB:P00550}.
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DR EMBL; AE016826; AAO27220.1; -; Genomic_DNA.
DR RefSeq; WP_011091621.1; NC_004545.1.
DR AlphaFoldDB; Q89A36; -.
DR SMR; Q89A36; -.
DR STRING; 224915.bbp_517; -.
DR EnsemblBacteria; AAO27220; AAO27220; bbp_517.
DR GeneID; 56471051; -.
DR KEGG; bab:bbp_517; -.
DR eggNOG; COG2213; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_028721_1_0_6; -.
DR OMA; GWAIKRF; -.
DR OrthoDB; 554815at2; -.
DR Proteomes; UP000000601; 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; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..640
FT /note="PTS system mannitol-specific EIICBA component"
FT /id="PRO_0000186613"
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..343
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 379..475
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 496..638
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 385
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT ACT_SITE 556
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT SITE 540
FT /note="Stabilizes the transition state in the phosphoryl
FT transfer from HPr to EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT MOD_RES 385
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00422"
FT MOD_RES 556
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550"
SQ SEQUENCE 640 AA; 70759 MW; A5B76D06E6909C3B CRC64;
MSVPMTVKVQ NLGRFLSAMI MPNISVFIAW GIISGLFIKS GWCPNQTLEK VLSPISVYLF
PILIANTGGY LINGKRGAIV GSIAVVGAII STAIPMLLGA MIIGPIGGWI TYYFDKISKY
KVKSGFEMLV NNFSVGILGV LLLFISFLCI GPMIEKLSCF LGYVVNLMIN NHLLPFIAIL
IEPAKIFFLN NVINHGVLFP LGIQEVVKFN KSIFFLIESN PGPGIGVLMA WFFFGCDNIK
KSLKEAIVIQ LFGGIHEIYF PYVLKNPRLI LALILGSITG IFILIVLRGG LISAASPGSI
ISILAMTPKG LYVINLLAII ISFLVSFLVS CMLLKISNRN HYVKGSNTKI EKDNFLINSS
FQKNRTCIKS SLDSHKCIRN IIFACDAGMG SSAVAAGILR NKIHDLNIFN ITVSNAAIDS
IPNFGVDLII THYSLTDRAR KRNSNAKHLS LNSFLDNAFY NELSKYLVEN NLDNNSSILD
FSVRNQNNFS SKKNVFSLTK ENIFLGQIAS SKEEVIRFIG RQLVNQGYVK EEYIEAMLER
EKMMSTWLGE SIALPHGTIQ SKDFILNTGI IFCQFPNGIL FGDDPEDIAH LVIGVAARNN
EHIPVVSNIT NILDNNDVIK SLSITKNIDD VLYLFSRKNI
