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Database: UniProt
Entry: A0A143XB44_9ACTN
LinkDB: A0A143XB44_9ACTN
Original site: A0A143XB44_9ACTN 
ID   A0A143XB44_9ACTN        Unreviewed;       936 AA.
AC   A0A143XB44;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Glucokinase {ECO:0000313|EMBL:CVH80231.1};
DE            EC=2.7.1.2 {ECO:0000313|EMBL:CVH80231.1};
GN   Name=glcK {ECO:0000313|EMBL:CVH80231.1};
GN   ORFNames=BN3658_02796 {ECO:0000313|EMBL:CVH80231.1};
OS   Coriobacteriaceae bacterium CHKCI002.
OC   Bacteria; Actinomycetota; Coriobacteriia; Coriobacteriales;
OC   Coriobacteriaceae.
OX   NCBI_TaxID=1780377 {ECO:0000313|EMBL:CVH80231.1, ECO:0000313|Proteomes:UP000199067};
RN   [1] {ECO:0000313|Proteomes:UP000199067}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Millard A.;
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; FCNB01000256; CVH80231.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A143XB44; -.
DR   STRING; 1780377.BN3658_02796; -.
DR   OrthoDB; 9810372at2; -.
DR   Proteomes; UP000199067; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005267; F:potassium channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR003280; 2pore_dom_K_chnl.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR000600; ROK.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR18964:SF177; N-ACETYLMANNOSAMINE KINASE; 1.
DR   PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF00480; ROK; 1.
DR   PRINTS; PR01333; 2POREKCHANEL.
DR   PRINTS; PR00169; KCHANNEL.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:CVH80231.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199067};
KW   Transferase {ECO:0000313|EMBL:CVH80231.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        51..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        215..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        312..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        344..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        374..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          21..238
FT                   /note="Ion transport"
FT                   /evidence="ECO:0000259|Pfam:PF00520"
FT   REGION          470..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   936 AA;  96979 MW;  6CADD333DD9E40FF CRC64;
     MRERIFNIVQ RARPGDVVSH AYDVFIVAVA FLSIVPLMFR PQDMTPQMAV VLNMIDVVTV
     YLLFLDYILR WMTHDFKVGK TGKLGKGGWR VFARYPFTPL AIIDMLAILP SLGVLPESLK
     FLRVLRVTKM FRYSKNLTIV ANVFRAQRNT LLSVLAVALM YIFVSGLVMF VNEPNTFDNF
     FDALYWATTA LTTVGYGDVY PVTDLGKFIS MASSLFGIAV IALPAGIITG GFLEQVRQRD
     EDAEAYFRAD ERDPFKGRTP FSYESVRAWA KAHPKAVAYG VTMLACVLVN EALYFAALAL
     GAPVWLDTVG TALAAVLLEP AAALIVGFAN NLVLAVQFGN AGNLLYYALS AITALVYGTV
     FARGRRITAR SLGWAALFLV VVEALISTVL TFSLAGGQLT TAAEQLYGSV LRGLGAPEAA
     AVFGALLVDK LADTVVVFAV AMGAVRLVVG SRLDPARWFS RSVVRAKGEE SAEARTGADD
     EAGTGVGASS DAEAPGGVCA EVRAFGDAGA CAGAGASGPA VGVASVVTAR ACEAGSAEAA
     GSTGSAGSAG SAGVAGSASA AEGVGAVGAA AGIGASGTAG DFGVESAAVT AIPSADAVGV
     ATASAAVAPE CVERYVLGID VGGTHTKAGV FDLAGSRVAS HAFGSQSVLA DGSHVRLSRE
     MRALLDQAGI DGRSVVGVGL AVPGAVAAEE SLTLCPHIDL DLRSYKSLLL ELFPRARVAV
     LNDADAAVLG DRWRGTSHDR QCENVALVTL GTGVGAGVVV RGRLLSGVHG AAGEVGHLCV
     NPSEEERCSC GKAGCLEQYA SATGLVRHAR AALLAAGDVA SSDQAADVFP DARAVLDAVE
     RRDPHARAAL DRFSDALGFG LAQMACFADP DVFVLGGGLS ERADLFIDAV RSRYRSCAVS
     ACRDTPVVAS SLGNECGVYG AAYRALQTLK DEGGLA
//
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