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Database: UniProt
Entry: F9SZJ0_9VIBR
LinkDB: F9SZJ0_9VIBR
Original site: F9SZJ0_9VIBR 
ID   F9SZJ0_9VIBR            Unreviewed;       650 AA.
AC   F9SZJ0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=IX91_01940 {ECO:0000313|EMBL:AIW12974.1};
OS   Vibrio tubiashii ATCC 19109.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW12974.1, ECO:0000313|Proteomes:UP000030071};
RN   [1] {ECO:0000313|EMBL:AIW12974.1, ECO:0000313|Proteomes:UP000030071}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW12974.1,
RC   ECO:0000313|Proteomes:UP000030071};
RA   Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT   "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT   tubiashii.";
RL   Submitted (AUG-2014) 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; CP009354; AIW12974.1; -; Genomic_DNA.
DR   RefSeq; WP_004742545.1; NZ_CP009354.1.
DR   AlphaFoldDB; F9SZJ0; -.
DR   STRING; 1051646.IX91_01940; -.
DR   KEGG; vtu:IX91_01940; -.
DR   PATRIC; fig|1051646.9.peg.366; -.
DR   eggNOG; COG2213; Bacteria.
DR   eggNOG; COG4668; Bacteria.
DR   HOGENOM; CLU_028721_1_0_6; -.
DR   Proteomes; UP000030071; Chromosome 1.
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..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        162..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        247..265
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        271..292
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          384..475
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          505..647
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   650 AA;  68608 MW;  316B2739DD55E4E5 CRC64;
     MISPDAKIKI QNFGRFLSNM VMPNIGAFIA WGFITALFIP TGWLPNETLA AMVGPMITYL
     LPLLIGYTGG KLVGGDRGAV VGAITTMGVI VGTDIPMFMG AMMVGPLGGW AIKKFDNYID
     GKVKSGFEML VNNFSAGIIG MLCAILAFMF IGPFVKILSG GLAAGVNFLV SAHLLPLTSI
     FVEPAKILFL NNAINHGIFS PLGIQQASEA GQSIFFLIEA NPGPGLGILL AYMVFGKGTA
     RQTAGGASII HFFGGIHEIY FPYILMNPRL ILAAIAGGMT GVFVLVMFNA GIVSPASPGS
     IFAILLMTQK GSIVGVLASI AAATGVSFTV AALLMKTQTS TEEDGDKAAL EKATSQMKEM
     KSGAKSESTV NAQNKGNIDL ANVTSIIVAC DAGMGSSAMG ASMLRKKVQD AGLNIGVNNL
     AINSLTESAD IVITHKDLTD RARKHAPNAH HISLTNFLNS EMYNQLVTKL LAAQKGAAAN
     DEHNAKVSVL AANDDSYEPQ QPSVFQIAPE NIHLGLTASN KEDAIRFAGN KLVEMGYVEP
     EYVDAMFERE KLVPTYLGES IAVPHGTIEA KDKVKKTGIV ICQYPAGIQF TDDQGDVAKL
     VIGIAAKNDE HIQVITTITN ALDEPEAIET LTSTQDVAKI LNILGNPQAA
//
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