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Database: UniProt
Entry: D3AMK2_9CLOT
LinkDB: D3AMK2_9CLOT
Original site: D3AMK2_9CLOT 
ID   D3AMK2_9CLOT            Unreviewed;       425 AA.
AC   D3AMK2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Permease IIC component {ECO:0000256|PIRNR:PIRNR006351};
GN   ORFNames=CLOSTHATH_04852 {ECO:0000313|EMBL:EFC96950.1};
OS   Hungatella hathewayi DSM 13479.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=566550 {ECO:0000313|EMBL:EFC96950.1, ECO:0000313|Proteomes:UP000004968};
RN   [1] {ECO:0000313|EMBL:EFC96950.1, ECO:0000313|Proteomes:UP000004968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13479 {ECO:0000313|EMBL:EFC96950.1,
RC   ECO:0000313|Proteomes:UP000004968};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (JAN-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active -transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane.
CC       {ECO:0000256|PIRNR:PIRNR006351}.
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:EFC96950.1}.
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DR   EMBL; ACIO01000466; EFC96950.1; -; Genomic_DNA.
DR   RefSeq; WP_006775282.1; NZ_GG667720.1.
DR   AlphaFoldDB; D3AMK2; -.
DR   HOGENOM; CLU_029688_1_0_9; -.
DR   Proteomes; UP000004968; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR004501; PTS_EIIC_3.
DR   InterPro; IPR004796; PTS_IIC_cello.
DR   NCBIfam; TIGR00410; lacE; 1.
DR   PANTHER; PTHR33989; -; 1.
DR   PANTHER; PTHR33989:SF4; PTS SYSTEM N,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIC COMPONENT; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   PIRSF; PIRSF006351; PTS_EIIC-Cellobiose; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
DR   PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|PIRNR:PIRNR006351};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006351};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW   ECO:0000256|PIRNR:PIRNR006351};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006351}.
FT   TRANSMEM        36..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        75..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        111..129
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        135..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        177..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        239..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        280..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..356
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        363..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        389..408
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..407
FT                   /note="PTS EIIC type-3"
FT                   /evidence="ECO:0000259|PROSITE:PS51105"
FT   DOMAIN          31..423
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
SQ   SEQUENCE   425 AA;  45984 MW;  653A72503058BC20 CRC64;
     MNEKTTGFQD KLMKYMMPIA NWVEKNNWLQ AIKDGMIADI PVIIIGSIFL LPIALNNLIA
     SGPIHDFISA HMGVLTYAAG FTNDLLSIFA AFFIATALAK RYGVHNTQTG ITAIIVHLIL
     SAVSIEGGIS TEFLGASGLF TSIISGIMSV EITRFLIKHN VIIKLPSSVP PMVGESFASL
     IPLVVNVIVA VAIANISIAV TGLAFPAAIM KLLAPAINTM DTLPALLIVI FLTQFLWFFG
     LHGPSITSAV WAAFAIAYQA ENMANYASGA PVTHIFTYGL YYNFLQVAGS GLTLGLVLFM
     MKSKAKSFKS IGVASLVPSI FGINEPVIFG LPILLNPYMF IPFVFGPLLI TVLTYFSMKV
     GLVGYPVAAP PGFLPPGVGA FLTTYDWRSV VLVFVSLIIM ALIYYPFFKM MEKDELKREA
     QSEAE
//
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