ID A0A1S2HX04_9MICO Unreviewed; 518 AA.
AC A0A1S2HX04;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=protein-N(pi)-phosphohistidine--D-mannitol phosphotransferase {ECO:0000256|ARBA:ARBA00011909};
DE EC=2.7.1.197 {ECO:0000256|ARBA:ARBA00011909};
GN ORFNames=BIU96_00375 {ECO:0000313|EMBL:OII15488.1};
OS Curtobacterium sp. MCBA15_008.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898736 {ECO:0000313|EMBL:OII15488.1, ECO:0000313|Proteomes:UP000180168};
RN [1] {ECO:0000313|EMBL:OII15488.1, ECO:0000313|Proteomes:UP000180168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_008 {ECO:0000313|EMBL:OII15488.1,
RC ECO:0000313|Proteomes:UP000180168};
RA Chase A.B., Arevalo P., Polz M.F., Berlemont R., Martiny J.B.;
RT "Evidence for ecological flexibility in the cosmopolitan genus
RT Curtobacterium.";
RL Submitted (SEP-2016) 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OII15488.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MJGN01000001; OII15488.1; -; Genomic_DNA.
DR RefSeq; WP_071290638.1; NZ_MJGN01000001.1.
DR AlphaFoldDB; A0A1S2HX04; -.
DR STRING; 1898736.BIU96_00375; -.
DR OrthoDB; 9814222at2; -.
DR Proteomes; UP000180168; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; 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 CDD; cd05567; PTS_IIB_mannitol; 1.
DR Gene3D; 3.40.50.2300; -; 1.
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; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
DR PROSITE; PS51104; PTS_EIIC_TYPE_2; 1.
PE 4: Predicted;
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 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..137
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..317
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 337..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 26..373
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT DOMAIN 428..518
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT REGION 394..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 394..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 518 AA; 53422 MW; 4282A6E7DB10D0DB CRC64;
MTTSSVAAPD APAKSRGGAR VAVQKFGTFL SGMVMPNIAI FIAWGIITAF FIETGWTPVG
ILGGFGETGG VANVGLVGPI LTYLIPLAIA IQGGRMVYET RGAVVGSIMT MGVIIGANGT
TMILGAMICG PLGAYLIKQI DKIWDGKIKP GFEMLVNNYA AGILGFGLAM VGFFWLAPLF
KLIAEGLGDA VNFLVQHSLL PLASVIIEPA KVFFLNNAIN HGVLDQLGAQ QVQESGKSIL
FLLEANPGPG LGILLAFTFF GVGIARSTAP GAIIIQFLGG IHEIYFPYVL QKPILFIAVI
LGGATGVATN VAFHSGLVAP ASPGSIFAVL GATAKDSFLG VILSVILSAA VSFAVASFFL
IATRKRDLAS GTGGDMSAAM AKLQANKGRD VNSATSGLLG NNSPANEQES EAALGGVGAG
TATATKVHNV VFACDAGMGS SAMGASVLRN KVKKAGIEGV TVVNKAIANL TGDEDLIITQ
EELTDRAKQK NPNAQHVSVG NFMNAPQYDQ VVEQLKNQ
//
