ID A0A1S2HZ52_9MICO Unreviewed; 517 AA.
AC A0A1S2HZ52;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=BIV00_13790 {ECO:0000313|EMBL:OII16815.1};
OS Curtobacterium sp. MCBA15_012.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1898738 {ECO:0000313|EMBL:OII16815.1};
RN [1] {ECO:0000313|EMBL:OII16815.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCBA15_012 {ECO:0000313|EMBL:OII16815.1};
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:OII16815.1}.
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DR EMBL; MJGP01000028; OII16815.1; -; Genomic_DNA.
DR RefSeq; WP_071248445.1; NZ_CP126267.1.
DR AlphaFoldDB; A0A1S2HZ52; -.
DR STRING; 1898738.BIV00_13790; -.
DR OrthoDB; 9814222at2; -.
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 26..52
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..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..361
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT DOMAIN 427..517
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
SQ SEQUENCE 517 AA; 53208 MW; 6C020662E88ABDCF CRC64;
MTTSSVAAPD APAKSRGGAR VAVQKFGTFL SGMVMPNIAI FIAWGLITAF FIEKGWTPVG
VLGGFGETNG VANIGLVGPI LTYLIPLAIA FQGGRMIYET RGAVVGSIMA MGVIIGANGT
IMILGAMVCG PLGAWLIKQI DKIWDGKIKP GFEMLVNNYA AGILGFVLAL IGFFLLAPLF
KAIAEGLGAA VKFLVDNSLL PVASIIIEPA KVFFLNNAIN HGVLDQLGAQ QVQESGKSIL
FLLEANPGPG LGILLAFTFF GVGIARSTAP GAILIQFLGG IHEIYFPYVL QKPVLFLAVI
LGGATGVATN VAFQSGLAAP ASPGSIIAVL TVTAKGSFVG VILSVILSAA VSFAVASFFL
LASRKRDLAN GGGDMSAAMA KLQANKGRDV NAATSGLLGT NAPATDEEAE ATLGGVGSAT
TTATRVQNVV FACDAGMGSS AMGASVLRNK VKKAGIEGVT VVNKAIANLD GTEDLVITQE
ELTDRAKQKV PNAQHVSVGN FMNAPQYDQV VDQLKNQ
//
