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Database: UniProt
Entry: A0A0X8D597_9BACL
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ID   A0A0X8D597_9BACL        Unreviewed;       483 AA.
AC   A0A0X8D597;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   SubName: Full=PTS sugar transporter {ECO:0000313|EMBL:AMA73638.1};
GN   ORFNames=ACH33_12750 {ECO:0000313|EMBL:AMA73638.1};
OS   Aneurinibacillus sp. XH2.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC   Aneurinibacillus group; Aneurinibacillus.
OX   NCBI_TaxID=1450761 {ECO:0000313|EMBL:AMA73638.1, ECO:0000313|Proteomes:UP000065566};
RN   [1] {ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|Proteomes:UP000065566};
RA   Xi L.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMA73638.1, ECO:0000313|Proteomes:UP000065566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Xh2 {ECO:0000313|EMBL:AMA73638.1,
RC   ECO:0000313|Proteomes:UP000065566};
RA   Zhang Z., Qiao N., Zhang Y., Xiao Z., Jing L., Zhao J.-Y.;
RT   "Draft genome of the novel themophilic polyhydroxyalkanoates producer
RT   Aneurinibacillus sp. XH2 (CCTCC M 2013550) isolated from Gudao oilfield in
RT   China.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP014140; AMA73638.1; -; Genomic_DNA.
DR   RefSeq; WP_057899365.1; NZ_CP014140.1.
DR   AlphaFoldDB; A0A0X8D597; -.
DR   STRING; 1450761.ACH33_12750; -.
DR   KEGG; anx:ACH33_12750; -.
DR   Proteomes; UP000065566; Chromosome.
DR   GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015572; F:N-acetylglucosamine transmembrane transporter activity; IEA:InterPro.
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; IPR010974; PTS_IIBC_nag.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR01998; PTS-II-BC-nag; 1.
DR   PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR   PANTHER; PTHR30009:SF4; PTS SYSTEM N-ACETYLGLUCOSAMINE-SPECIFIC EIICBA 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:UP000065566};
KW   Sugar transport {ECO:0000256|ARBA:ARBA00022597,
KW   ECO:0000313|EMBL:AMA73638.1}; 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        15..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        48..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        77..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        108..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        147..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        175..195
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        241..261
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        273..291
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        297..320
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        351..371
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..383
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   DOMAIN          402..483
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   ACT_SITE        424
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   483 AA;  52364 MW;  36F34ADEACCA082D CRC64;
     MMNVLSALQK IGRLLMMPIA VLPAAAILLG IGAMKFQNPF MAHLAKIFSA GGGAILGNLP
     MLFAIGVAIG LTDGAGVAGL AATLGYFVLT NVLNVFDVIG PNGEKIVHLD MGVIGGIITG
     AVTAFLYRRY KDIRLPQALG FFSGSRFVPI VTALVMVVFG VVMGYVWLPV QNGIHALGMW
     IVSAGGIGMF LYGLLNRLLI PFGLHHILNS ITWFQIGEFT NVAGDVFHGD LSRYFAGDKT
     AGMFMTGFFP IMMFGLPAAC IAMVKEAKPE KRAFVSSVLL SAAFASFLTG VTEPIEFSFM
     FLAPLLFIIH AILTGLFMAF TYLSGMHLGF GFSAGFIDYV LNWHLATKPW LLIPFGAACF
     IVYYFVFRFF IRMFDLKTPG RDEVPTESGT TFKEEGNALE MKERAMSILP LIGGVENIRN
     IDACITRLRL IVGDDSLVKD EELKKLGAAG VMRLGKGNVQ IVFGTESELI KEEIKSLLNQ
     SAS
//
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