ID A0A0A6YCU2_9MICC Unreviewed; 691 AA.
AC A0A0A6YCU2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=GY22_05590 {ECO:0000313|EMBL:KHD98032.1};
OS Kocuria polaris.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Kocuria.
OX NCBI_TaxID=136273 {ECO:0000313|EMBL:KHD98032.1, ECO:0000313|Proteomes:UP000030466};
RN [1] {ECO:0000313|EMBL:KHD98032.1, ECO:0000313|Proteomes:UP000030466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMS 76or {ECO:0000313|EMBL:KHD98032.1,
RC ECO:0000313|Proteomes:UP000030466};
RX PubMed=12656171; DOI=10.1099/ijs.0.02336-0;
RA Reddy G.S., Prakash J.S., Prabahar V., Matsumoto G.I., Stackebrandt E.,
RA Shivaji S.;
RT "Kocuria polaris sp. nov., an orange-pigmented psychrophilic bacterium
RT isolated from an Antarctic cyanobacterial mat sample.";
RL Int. J. Syst. Evol. Microbiol. 53:183-187(2003).
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}.
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:KHD98032.1}.
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DR EMBL; JSUH01000004; KHD98032.1; -; Genomic_DNA.
DR RefSeq; WP_035924838.1; NZ_JSUH01000004.1.
DR AlphaFoldDB; A0A0A6YCU2; -.
DR OrthoDB; 9814222at2; -.
DR Proteomes; UP000030466; Unassembled WGS 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};
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 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 295..318
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 338..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..368
FT /note="PTS EIIC type-2"
FT /evidence="ECO:0000259|PROSITE:PS51104"
FT DOMAIN 417..512
FT /note="PTS EIIB type-2"
FT /evidence="ECO:0000259|PROSITE:PS51099"
FT DOMAIN 550..689
FT /note="PTS EIIA type-2"
FT /evidence="ECO:0000259|PROSITE:PS51094"
FT REGION 371..409
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 522..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 70516 MW; D59907786AD036E9 CRC64;
MATATTSETT APAGGRSTAA RAHVQRFGTF LSGMIMPNIG AFIAWGLITA FFIEAGFTPF
GPLGGFGENA EGEPYTGLVG PMITYLLPLL IAYTGGRMVY DVRGGVVGAI ATMGVIVGTD
IPMFIGAMLM GPLTAWVMKK VDAIWDGKIK PGFEMLVNNF SAGILAAAMA IFGFFLIGPA
VLAFSNAAAS AVDFLVTRGL LPLTSIFIEP AKVLFLNNAI NHGILTPLGT AQALEEGKSI
LFLLEANPGP GLGILLAYTV FGRGAARASA PGAALIHFVG GIHEIYFPYV LMKPALILAA
IAGGMTGIFT LTLFDAGLRA PAAPGSIIAI FAQATTDSYV GVALAVTAAT AVSFFVASII
LKASKDKGEG DLTEATSRME GMKGKKSSVS SAIVGTSGGA DTGGTPAREL ADGGPVQRIV
FACDAGMGSS AMGASVLRNK VKAAGFADVK VTNAAIANLT DDFDIVVTHQ DLATRARPKV
PSAAVVTVDN FMGSPRYDEI VEAVQQRNGA AVPAGGGAAA ATAGGGGAAS GGDTVAADPG
EGAGTSGDAT ILTRDRIVMD GGARNAAQAI DEAGGLLVAA GAVTDAYVAS MHEREESVST
FMGNGLAIPH GTNQAKDSIR SSALSVVRYP EGLDWNGKPV TWVIGIAGKD NEHLAILSRV
AKIFGNKEKV RQLDEARTAD EVLDLLGKVN D
//
