ID A0A0G0VCQ8_9BACT Unreviewed; 789 AA.
AC A0A0G0VCQ8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE SubName: Full=Cell division protein FtsK/SpoIIIE {ECO:0000313|EMBL:KKR60512.1};
GN ORFNames=UT97_C0001G0083 {ECO:0000313|EMBL:KKR60512.1};
OS Parcubacteria group bacterium GW2011_GWC2_40_31.
OC Bacteria.
OX NCBI_TaxID=1618924 {ECO:0000313|EMBL:KKR60512.1, ECO:0000313|Proteomes:UP000034205};
RN [1] {ECO:0000313|EMBL:KKR60512.1, ECO:0000313|Proteomes:UP000034205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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:KKR60512.1}.
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DR EMBL; LBYV01000001; KKR60512.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0VCQ8; -.
DR STRING; 1618924.UT97_C0001G0083; -.
DR PATRIC; fig|1618924.3.peg.89; -.
DR Proteomes; UP000034205; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.30.980.40; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR025199; FtsK_4TM.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR018541; Ftsk_gamma.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF13491; FtsK_4TM; 1.
DR Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:KKR60512.1};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 390..579
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 737..789
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..246
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 750..769
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407..414
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 789 AA; 86724 MW; 0C3275C2BCA308BC CRC64;
MSSKSKAKKQ KIKHKKEEEK EEDEPKESFL NALEDRTKNF IISIVLFSFG TVFTLSYFNK
AGPAGKYINN IFDSLFGNGS ILLPLALFAS AGILALSIKP SFLKRTLIGI AVFLIGNLGI
MATIWGKDAG GYIGYLTSLP LMKLFDFWAS IIILSAILVV SATLIINKPI FAFIPFKLKR
READDDIIQA NHFNENGGAV EEKENAKESA HVPAESGAGK AMEIKKDKKR KEGTGKDKEE
EYEEGSISYP KQNKVAFIPP PLELLEGDRG KPSSGDIKAN ANIIKRTLQN FGIDVEMGEI
NIGPSVTQYT LKPAEGVKLA RIVALQNDLA LSLAAHPIRI EAPIPSRSLV GIEIPNSTKT
IIGLATLFKE SDYQNGTHPL LVTFGRSVGG QAAFYNLAKM PHLLVAGATG SGKSIYIHSL
IMSLLYRNSP EDLRFIMIDP KRVELTVYNK IPHMLTPVIT ETKKAILILK WLTKEMERRY
DTLLSAGVRN IESYRKEEAS DKKPMPYLVV VIDELADLMS TYPREMEASI VRLAQMSRAV
GIHLVLSTQR PSVEVITGLI KANVPSRVAL QVASQIDSRT ILDMSGAEKL LGNGDMLYLV
GDSAKPRRVQ GPYVTDKEIK NVVDFLADTY KDFDLEDIDT SAENGGSPSK ARGAISIDLD
QVGMDEDADD EMYEEARATV IEFGKASTSF LQRKLKVGYA RAARLMDMLE ERGIISQGDG
AKPRQVLVES RDAFADAVDD YKDENGSKTD GSEQINQQES VSTFPTSPSE AGLADKDADQ
NIEKNGNQN
//
