ID A0A090IM65_9GAMM Unreviewed; 650 AA.
AC A0A090IM65;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 Name=mtlA {ECO:0000313|EMBL:CED70338.1};
GN ORFNames=AWOD_I_0243 {ECO:0000313|EMBL:CED70338.1};
OS Aliivibrio wodanis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Aliivibrio.
OX NCBI_TaxID=80852 {ECO:0000313|EMBL:CED70338.1, ECO:0000313|Proteomes:UP000032427};
RN [1] {ECO:0000313|Proteomes:UP000032427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=06/09/139 {ECO:0000313|Proteomes:UP000032427};
RA Hjerde E.;
RL Submitted (SEP-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; LN554846; CED70338.1; -; Genomic_DNA.
DR RefSeq; WP_045101048.1; NZ_LN554846.1.
DR AlphaFoldDB; A0A090IM65; -.
DR STRING; 80852.AWOD_I_0243; -.
DR GeneID; 28539772; -.
DR KEGG; awd:AWOD_I_0243; -.
DR PATRIC; fig|80852.17.peg.249; -.
DR HOGENOM; CLU_028721_1_0_6; -.
DR OrthoDB; 9814222at2; -.
DR Proteomes; UP000032427; Chromosome 1 complete sequence.
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, ECO:0000313|EMBL:CED70338.1};
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 97..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 157..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 270..291
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 311..334
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 13..344
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; 68805 MW; D69ABFC1AB977F94 CRC64;
MISPDAKIKI QNFGRFLSNM VMPNIGAFIA WGFITALFIP TGWIPNEALA KLVGPMITYL
LPLLIGYTGG KLVGGERGAI VGAITTMGVI AGTDIPMFMG AMMVGPMGGL AIKLFDQKVD
GKIKSGFEML VNNFSAGIIG MLCAIVAFYF IGPFVKVLSA GLAGGVNFLV EAGLLPLTSI
FVEPAKILFL NNAINHGIFS PLGIQQANDV GQSIFFLIEA NPGPGLGILL AYMFFGKGSA
KQTAGGASII HFFGGIHEIY FPYILMNPRL ILAAIAGGMT GVFVLTLFNA GMVAPASPGS
IFAILLLTPK ASAIGVICSI LSATAVSFTV AALLMKMQTT SDEDDGTSLD DATAAMRDMK
SGSKGKASGI TAEKSNSPKL NNIQKIIVAC DAGMGSSAMG AGLLRKKVQA AGLNISVTNC
AINNLPTDVD IVITHKDLTD RARKHAENAE HISLTNFLDS HIYNDLVARI MASTYPEAAN
DDEIPQVSPV AANDEFFEPQ KAQPFQIEEK NIHLGLTFKT KEEAIQYAGE QLVSLGYAEP
EYVAAMFDRE KLVPTYLGES IAVPHGTIEA KDRVIKTGIV ICQYPSGVQF TEDEDDVAKL
VIGIAAKNDE HIQVITSITN ALDEPGAIEK LTSTNSVSEI LEILSGEQAA
//
