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Database: UniProt
Entry: A0A1Q4ZNJ9_9ACTN
LinkDB: A0A1Q4ZNJ9_9ACTN
Original site: A0A1Q4ZNJ9_9ACTN 
ID   A0A1Q4ZNJ9_9ACTN        Unreviewed;       520 AA.
AC   A0A1Q4ZNJ9;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=PTS alpha-glucoside transporter subunit IIA {ECO:0000313|EMBL:OKI48389.1};
GN   ORFNames=A6A29_05050 {ECO:0000313|EMBL:OKI48389.1};
OS   Streptomyces sp. TSRI0281.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI48389.1, ECO:0000313|Proteomes:UP000186952};
RN   [1] {ECO:0000313|EMBL:OKI48389.1, ECO:0000313|Proteomes:UP000186952}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI48389.1,
RC   ECO:0000313|Proteomes:UP000186952};
RX   PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA   Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA   Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA   Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT   "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL   MBio 7:e02104-e02116(2016).
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:OKI48389.1}.
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DR   EMBL; LWLE01000001; OKI48389.1; -; Genomic_DNA.
DR   RefSeq; WP_073718663.1; NZ_LWLE01000001.1.
DR   AlphaFoldDB; A0A1Q4ZNJ9; -.
DR   STRING; 1718998.A6A29_05050; -.
DR   OrthoDB; 9797715at2; -.
DR   Proteomes; UP000186952; 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:UP000186952};
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        135..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        168..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        253..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        298..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        333..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        445..466
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..90
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          130..482
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   REGION          483..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        30
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   520 AA;  52660 MW;  CD4D53A20D5EE885 CRC64;
     MATEDKNRAT AAAILPLVGG AANVSSIAHC MTRLRLGLHD RSLVDDEALK AVPAVMGVVD
     DDTYQIVLGP GTVARVTPEF EKLVEEGRAA APEPAPATGP VSADELAAQG AAIKAQQKAK
     NATPFKLFLR KIANIFVPLI PALIGCGIIA GLNGLLVNLE WLPSVTPALA AMASGFMALI
     AVFVGYNTAK EFGGTPILGG AVAAIIVFPG VANIDAFGQT LSPGQGGVLG ALGAAVLAVY
     VEKWCRRWVP EALDVLVTPT LTVLISGLVT IFGLMYVAGE VSSAIGTFAD WLLSNGGAGA
     GFVLGGLFLP LVMLGLHQAL IPIHTTLIEQ QGYTVLLPIL AMAGAGQVGA AAAVYFRLPR
     NESIRRTIKS ALPAGLLGVG EPLIYGVSLP LGRPFITACV GGAFGAGFVG LFNQLGDTVG
     STAIGPSGWA LFPLLDGNHG LGSTIAIYAG GLLVGYVAGF LATYFFGFSK DLLTEFNVSQ
     EPAPSAVTAT GGHPAAAPGS APGSGPETGP GSPAKEPAGV
//
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