PTM3C_BUCAI
ID PTM3C_BUCAI Reviewed; 632 AA.
AC P57635;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=BU572;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(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-548 and
CC Cys-380. {ECO:0000250|UniProtKB:P00550}.
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DR EMBL; BA000003; BAB13262.1; -; Genomic_DNA.
DR RefSeq; NP_240376.1; NC_002528.1.
DR RefSeq; WP_009874520.1; NC_002528.1.
DR AlphaFoldDB; P57635; -.
DR SMR; P57635; -.
DR STRING; 107806.10039228; -.
DR EnsemblBacteria; BAB13262; BAB13262; BAB13262.
DR KEGG; buc:BU572; -.
DR PATRIC; fig|107806.10.peg.575; -.
DR eggNOG; COG2213; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_028721_1_0_6; -.
DR OMA; GWAIKRF; -.
DR Proteomes; UP000001806; 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..632
FT /note="PTS system mannitol-specific EIICBA component"
FT /id="PRO_0000186611"
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..341
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00427"
FT DOMAIN 374..469
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00422"
FT DOMAIN 488..630
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00417"
FT ACT_SITE 380
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT ACT_SITE 548
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00417"
FT SITE 532
FT /note="Stabilizes the transition state in the phosphoryl
FT transfer from HPr to EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550"
FT MOD_RES 380
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P00550,
FT ECO:0000255|PROSITE-ProRule:PRU00422"
FT MOD_RES 548
FT /note="Phosphohistidine; by HPr"
FT /evidence="ECO:0000250|UniProtKB:P00550"
SQ SEQUENCE 632 AA; 69974 MW; DC413636A0BFF552 CRC64;
MLTLIKLKIQ NFGRFLSNMI MPNISIFIAW GMMNALFMPL GWQPNKTLEQ LISPMIFYLL
PILIGYTGGS LISGSRGGLI GSITTIGVIT STNIPMLLGA MISGPLGGWT IKYFDKKIEN
KVKNGFEMLV NNFSLAILGI LLAIISFFTI GPFIEWVSYF LGTLIQIILS YNLLPLTSII
IEPAKIFFLN NVINHGIFSP LGIQDALDKN HSIFFLIESN PGPGLGLLIA WFFFGKGELS
KSSGGAALIE FFGGIHEIYF PYVLIKPKLI IPLILGGMSG IFILVLLHGG LISTASPGSI
LSILAMTPKG LYFSNIISVA CSFLVSFISS SILLKYDFNT IQKDSNYTVK QGKNSFNSKT
SREDFNNFNF SKIKTIIVAC DAGMGSSAMG ASILRKKIKN ANLNHISVLN MAINALPQDA
DLIITHQNLT NRAKDNAPFS QHISLKNFLN NHFYDNLVKK LVENMVFLYD NHTDSVNKYT
QQKKDALFQL NEENIILNQY ASNKEEAINI VGKHLVKQGY VKFDYIDSML EREKMASTWL
GESIALPHGT IEAKDSVLKT GIIFCQFPKG VRFGEDVDDI AYLVIGIAAK NNEHIMVVSN
ITNALDKKDT IQRLSHTTSI KEALSLLTME KI
