ID A1SLI1_NOCSJ Unreviewed; 668 AA.
AC A1SLI1;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=PTS system mannitol-specific EIICBA component {ECO:0000256|ARBA:ARBA00015039};
DE EC=2.7.1.197 {ECO:0000256|ARBA:ARBA00011909};
DE AltName: Full=EIICBA-Mtl {ECO:0000256|ARBA:ARBA00030684};
GN OrderedLocusNames=Noca_3164 {ECO:0000313|EMBL:ABL82666.1};
OS Nocardioides sp. (strain ATCC BAA-499 / JS614).
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=196162 {ECO:0000313|EMBL:ABL82666.1, ECO:0000313|Proteomes:UP000000640};
RN [1] {ECO:0000313|Proteomes:UP000000640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Thompson L.S., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Mattes T., Gossett J.,
RA Richardson P.;
RT "Complete sequence of chromosome 1 of Nocardioides sp. JS614.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABL82666.1, ECO:0000313|Proteomes:UP000000640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-499 / JS614 {ECO:0000313|Proteomes:UP000000640};
RX PubMed=21551312; DOI=10.1128/JB.05109-11;
RA Coleman N.V., Wilson N.L., Barry K., Brettin T.S., Bruce D.C., Copeland A.,
RA Dalin E., Detter J.C., Del Rio T.G., Goodwin L.A., Hammon N.M., Han S.,
RA Hauser L.J., Israni S., Kim E., Kyrpides N., Land M.L., Lapidus A.,
RA Larimer F.W., Lucas S., Pitluck S., Richardson P., Schmutz J., Tapia R.,
RA Thompson S., Tice H.N., Spain J.C., Gossett J.G., Mattes T.E.;
RT "Genome Sequence of the ethene- and vinyl chloride-oxidizing actinomycete
RT Nocardioides sp. strain JS614.";
RL J. Bacteriol. 193:3399-3400(2011).
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:0000256|ARBA:ARBA00001655};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000509; ABL82666.1; -; Genomic_DNA.
DR RefSeq; WP_011756600.1; NC_008699.1.
DR AlphaFoldDB; A1SLI1; -.
DR STRING; 196162.Noca_3164; -.
DR KEGG; nca:Noca_3164; -.
DR eggNOG; COG2213; Bacteria.
DR eggNOG; COG4668; Bacteria.
DR HOGENOM; CLU_028721_1_0_11; -.
DR OrthoDB; 9814222at2; -.
DR Proteomes; UP000000640; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 CDD; cd00211; PTS_IIA_fru; 1.
DR CDD; cd05567; PTS_IIB_mannitol; 1.
DR Gene3D; 3.40.50.2300; -; 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 PANTHER; PTHR30181; MANNITOL PERMEASE IIC COMPONENT; 1.
DR PANTHER; PTHR30181:SF2; PTS SYSTEM MANNITOL-SPECIFIC EIICBA COMPONENT; 1.
DR Pfam; PF00359; PTS_EIIA_2; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR SUPFAM; SSF52794; PTS system IIB component-like; 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 4: Predicted;
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Reference proteome {ECO:0000313|Proteomes:UP000000640};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 74..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 168..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 246..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 279..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 302..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 344..369
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 21..377
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT DOMAIN 413..505
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 525..665
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
SQ SEQUENCE 668 AA; 69730 MW; 444EB8E1768E3939 CRC64;
MATATQTPAE RTSTRVHVQR FGTFLSNMVM PNIGAFIAWG LITAMFIEVG WLNLGGGDHG
WLGPGSWVAH IGGWGDYAGG GIVGPMITYL LPVLIGYTGG KMVYNDLVRG GVVGAIATFG
VIAGTSVPMF MGAMIMGPLA GWSMKKIDST WDGKIKPGFE MLVDNFSAGI WGGILATFGF
FALSDVLTWI SDRLGDGVEF LVEHDLLPFA SFVIEPAKVL FLNNALNHGV LTPLGLAESA
DSGKSILFLL EANPAAGIGL LLAYSIFGKG LAKASAPGAA IIHFFGGIHE VYFPFVLMKP
KLILAMIAGG FTQILINVIF SSGLRSPAAP GSVFAVYISA PTDLRNLTGV TLSILGGAAA
SFFVAAILLK TDKTIEAEDE LVSATANMEA MKGKKSIASS LVGSSTAHSG AITSIVFACD
AGMGSSAMGA SVLRKKIHGA GFTDVTVVNK AIANLTDSYD LVVTHQDLTD RARLKTGSAI
QVSVENFMGS PRYDEIVELV RERNGGAAPA SVGSADAEEP ALAGGLLADD AIVLDAPAGE
SRDAAITRAG ELLLASGAAT RAYVEAMHTR EGSVSTAMGN LLAIPHGTNE AKTEVSRTAL
SFVRYPEPID WNGKPVRYVV GIAAMGNEHL KLLGRIAEVF VDPEQVRRLE EAGSAADVRA
VLGEVQPV
//
