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Database: UniProt
Entry: W1Q658_ABIDE
LinkDB: W1Q658_ABIDE
Original site: W1Q658_ABIDE 
ID   W1Q658_ABIDE            Unreviewed;       463 AA.
AC   W1Q658;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=PTS system sucrose-specific IIBC component {ECO:0000313|EMBL:ESK65714.1};
GN   ORFNames=GCWU000182_000779 {ECO:0000313|EMBL:ESK65714.1};
OS   Abiotrophia defectiva ATCC 49176.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX   NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK65714.1, ECO:0000313|Proteomes:UP000019050};
RN   [1] {ECO:0000313|EMBL:ESK65714.1, ECO:0000313|Proteomes:UP000019050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK65714.1,
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:ESK65714.1}.
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DR   EMBL; ACIN03000005; ESK65714.1; -; Genomic_DNA.
DR   AlphaFoldDB; W1Q658; -.
DR   STRING; 592010.GCWU000182_000779; -.
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: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; IPR010973; PTS_IIBC_sucr.
DR   NCBIfam; TIGR01996; PTS-II-BC-sucr; 1.
DR   PANTHER; PTHR30175:SF7; NEGATIVE REGULATOR OF SACY ACTIVITY; 1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 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        111..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        153..173
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        185..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        255..275
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        295..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        337..360
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        394..414
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        434..455
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          4..87
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          106..463
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   ACT_SITE        26
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   463 AA;  49699 MW;  B57B9B0FD467EFBD CRC64;
     MGFKEIAQDV VKYLGGKENI SSVAHCATRL RVMVKDEAKI DKEAIENTDK VMGAFFNSGQ
     YQIIFGTGTV NKVYEEVSAL GVNAVTKSDQ KEEVKPQGNV LQRMIRTFGD VFVPIIPVLV
     ATGLFMGVRG VLTRPEVIGL FGLTDPKQID QNFLLYTQIL TDTAFAFLPA LVAWSSFKVF
     GGNPVLGIVL GLMMVNPALP NAYAVASGDA QALTFFGFIP VVGYQGTVLP AFFVGLIGAK
     LEKWLHDHVK DTFDLIVTPF LTFLVMSILG LFAIGPVFHS LETVVLDVTK QILTLPFGLA
     GLIVGGVQQI IVVTGIHHIF NFLELQLLTN GDKTNPLNAY FTAAMAGQAG ATFAVGYKTV
     NHKVRALAYS SGISCLLGIT EPAIFGVNLR YGKPFVMGLV AGAAGGWLAG LFKLAATGMS
     VTVLPGVLLY LNNIFAYLLV LVVSFGIGFG LTYAFGYKED KQA
//
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