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Database: UniProt
Entry: W1Q1C6_ABIDE
LinkDB: W1Q1C6_ABIDE
Original site: W1Q1C6_ABIDE 
ID   W1Q1C6_ABIDE            Unreviewed;       503 AA.
AC   W1Q1C6;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=PTS system trehalose-specific IIBC component {ECO:0000313|EMBL:ESK64786.1};
GN   ORFNames=GCWU000182_001973 {ECO:0000313|EMBL:ESK64786.1};
OS   Abiotrophia defectiva ATCC 49176.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX   NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK64786.1, ECO:0000313|Proteomes:UP000019050};
RN   [1] {ECO:0000313|EMBL:ESK64786.1, ECO:0000313|Proteomes:UP000019050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK64786.1,
RC   ECO:0000313|Proteomes:UP000019050};
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 (JUN-2013) to the EMBL/GenBank/DDBJ databases.
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:ESK64786.1}.
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DR   EMBL; ACIN03000017; ESK64786.1; -; Genomic_DNA.
DR   RefSeq; WP_023392566.1; NZ_KI535342.1.
DR   AlphaFoldDB; W1Q1C6; -.
DR   STRING; 592010.GCWU000182_001973; -.
DR   GeneID; 84817043; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_012312_2_1_9; -.
DR   OrthoDB; 9769191at2; -.
DR   Proteomes; UP000019050; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0015574; F:trehalose transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   InterPro; IPR011296; PTS_IIBC_treh.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR01992; PTS-IIBC-Tre; 1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF4; PTS SYSTEM TREHALOSE-SPECIFIC EIIBC COMPONENT; 1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019050};
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        112..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        205..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        322..342
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        362..383
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        417..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        462..482
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..87
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          107..498
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   ACT_SITE        27
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   503 AA;  54767 MW;  E96FA3C698FD0F9E CRC64;
     MSNFKQDATQ LLSLIGGKEN ISAVTHCATR MRFALVDPSQ ADVKAIEALP SVKGSFTQAG
     QFQVIIGNAV SEFYKEFQAV SGVGEASKDE VKAAAKKNQS LLQRAMTTMA EIFAPIIPAI
     IVGGLILGFR NILENVPLEF LGQKFVDGQA QFNPDGTILY NTIVNVSQFW SGVNDFLWLP
     GEAIFHFLPV GIVWSVTRKM GTTQILGIVL GITLVSGRLT NAYEYAQAVK EQTVKFWDFG
     FFQLKAIGYQ AQVIPAILAG LALSYLEIFW RKVVPEVLSM ILVPFLALVP AVILAHTVLG
     PIGWTIGDWI SQVVRAGLTG TFSWLFGAIF GAFYAPLVIT GLHHMTNAID SELIARFNGT
     GLWPMIALSN IAQGSAVLAV WWLTRKDEEQ NQITVPSTIS CYLGVTEPAL FGVNLKYLYP
     FLAGMIGSSI AGLIATTYKV TSNAIGVGGL PGFLAIQPGS MAMFFVCMAV ALVVPFVVTL
     FFNRQFKFLE NKAIDFDIPF FNK
//
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