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Database: UniProt
Entry: A0A411WNA7_9GAMM
LinkDB: A0A411WNA7_9GAMM
Original site: A0A411WNA7_9GAMM 
ID   A0A411WNA7_9GAMM        Unreviewed;       658 AA.
AC   A0A411WNA7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 23.
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   ORFNames=EKN56_15280 {ECO:0000313|EMBL:QBH97647.1};
OS   Limnobaculum zhutongyuii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Budviciaceae; Limnobaculum.
OX   NCBI_TaxID=2498113 {ECO:0000313|EMBL:QBH97647.1, ECO:0000313|Proteomes:UP000293154};
RN   [1] {ECO:0000313|EMBL:QBH97647.1, ECO:0000313|Proteomes:UP000293154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF-458 {ECO:0000313|EMBL:QBH97647.1,
RC   ECO:0000313|Proteomes:UP000293154};
RA   Ge Y.;
RT   "Pragia sp. nov. isolated from the gut tract of Carduelis flavirostris.";
RL   Submitted (MAR-2019) to the EMBL/GenBank/DDBJ databases.
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; CP034752; QBH97647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A411WNA7; -.
DR   KEGG; prag:EKN56_15280; -.
DR   OrthoDB; 9814222at2; -.
DR   Proteomes; UP000293154; 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   InterPro; IPR004718; PTS_IIC_mtl.
DR   NCBIfam; TIGR00851; mtlA; 1.
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   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        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        49..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        80..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        270..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..335
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          13..342
FT                   /note="PTS EIIC type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51104"
FT   DOMAIN          389..481
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          513..655
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
FT   REGION          354..377
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   658 AA;  70228 MW;  8BDD888CD5D55C90 CRC64;
     MLSPNIKVKV QNFGRFLSNM VMPNIGAFIA WGLITALFIP TGWLPNETLA KLVGPMITYL
     LPLLIGYTGG RLIGDERGGV VGAITTMGVV IGADMPMFMG AMIVGPLGGY AIRRFDRWVD
     GKIKSGFEML VNNFSAGIIG MLLAILAFMA IGPLVESLSK LLAAGVNIMV QNNLLPLTSI
     FVEPAKILFL NNAINHGIFS PLGIQQATET GKSIFFLIEA NPGPGLGVLL TYMFFGKGSA
     KQSAPGAVII HFFGGIHEIY FPYVLMNPRL IIAVILGGMT GVFTLTLFNA GLVSPASPGS
     IFAVLLMTPK SSLIGVVLSI LASGIVSFLI SAVMLKRVPA GEEENNGLAD ATRRMQGMKQ
     QSKGNKAQGG AAQPAMHKGD MAKDLSYVRT IMVACDAGMG SSAMGAGVLR KKVKDAGLNH
     IAVANCAINS LPEGVDMVIT HQDLTRRAMD HAPHAIHISL KNFLDSQLYN DLTARLLAAK
     HPQAANDSKL ITQTIVAAND EHFDPANQEE NLFELGANNI FLNLQADNKE QAIRFAGQML
     VDGGYVEPDY VDAMLAREAL TSTYLGESIA VPHGTVEAKD RVLRTGVVIC QYPQGVCFGD
     TPEEIAHLVI GIAARNNQHI QVITRLTNAL DEDGIIERLA QTTSVQEVLD LLAGEQAA
//
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