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Database: UniProt
Entry: A0A0Q9AR87_9ACTN
LinkDB: A0A0Q9AR87_9ACTN
Original site: A0A0Q9AR87_9ACTN 
ID   A0A0Q9AR87_9ACTN        Unreviewed;       500 AA.
AC   A0A0Q9AR87;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=PTS sugar transporter subunit IIC {ECO:0000313|EMBL:KRD17714.1};
GN   ORFNames=ASE41_23100 {ECO:0000313|EMBL:KRD17714.1};
OS   Streptomyces sp. Root264.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1736503 {ECO:0000313|EMBL:KRD17714.1, ECO:0000313|Proteomes:UP000051177};
RN   [1] {ECO:0000313|EMBL:KRD17714.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRD17714.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRD17714.1, ECO:0000313|Proteomes:UP000051177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root264 {ECO:0000313|EMBL:KRD17714.1,
RC   ECO:0000313|Proteomes:UP000051177};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KRD17714.1}.
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DR   EMBL; LMIZ01000016; KRD17714.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q9AR87; -.
DR   STRING; 1736503.ASE41_23100; -.
DR   Proteomes; UP000051177; 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   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR   PANTHER; PTHR30175:SF3; PTS SYSTEM N-ACETYLMURAMIC ACID-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:UP000051177};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW   ECO:0000313|EMBL:KRD17714.1}; 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..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        144..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        197..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        233..258
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        278..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        313..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        375..395
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          110..462
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   REGION          461..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        472..500
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        26
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   500 AA;  49705 MW;  9C56BB91A1383A96 CRC64;
     MDSSSTAAAI LPLVGGPANV LSVAHCMTRL RLDLADPSRA DEEALRALPG VLGVVVADGA
     FQIVLGPGVV TRVTADFEQL TAAHRLAARG AGLKARQRER DATPLKSALR RLAAVFVPLV
     PALVGCGILA GANGLLLNAG LLPGLTPALT AVASGFMALI AVFVGHNTAK EFGGTPVLGG
     AVAAIVVYPG VAKVTAFGVT LAPGQGGVLG ALAAALLATY VEKQCRGRVP ETLDVLLTPA
     LTVLVAGLGT LYGLMYAAGA VSAAVGSAAN WLLTTTGAFA GLLLGGLFLP LVMLGLHQAL
     IPVHTTLIEQ QGYTVLLPVL AMAGAGQVGA AAAVYVRLRD DVALRTTIRS ALPAGLLGVG
     EPLIYGVSLP LGRPFLTACA GGAAGGAFIG FFAMLGDRVG ATAIGPSGWA LFPLLAGDRG
     PGTTAAVYAG GLLTGYAVGF AATYVFGGVR AAAAALSPTT TATAVDTAPP DNLGPFTPPE
     TTPRPDPATP PATTTAPPTH
//
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