ID A0A0G1YX65_9BACT Unreviewed; 713 AA.
AC A0A0G1YX65;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 08-NOV-2023, entry version 34.
DE SubName: Full=Cell division FtsK/SpoIIIE {ECO:0000313|EMBL:KKW47755.1};
GN ORFNames=UZ00_C0001G0011 {ECO:0000313|EMBL:KKW47755.1};
OS Parcubacteria group bacterium GW2011_GWA1_60_11.
OC Bacteria.
OX NCBI_TaxID=1618805 {ECO:0000313|EMBL:KKW47755.1, ECO:0000313|Proteomes:UP000034313};
RN [1] {ECO:0000313|EMBL:KKW47755.1, ECO:0000313|Proteomes:UP000034313}
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 -!- 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:KKW47755.1}.
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DR EMBL; LCSF01000001; KKW47755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1YX65; -.
DR PATRIC; fig|1618805.3.peg.11; -.
DR Proteomes; UP000034313; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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; IPR003593; AAA+_ATPase.
DR InterPro; IPR041027; FtsK_alpha.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR018541; Ftsk_gamma.
DR InterPro; IPR036259; MFS_trans_sf.
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; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF103473; MFS general substrate transporter; 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:0000313|EMBL:KKW47755.1};
KW Cell division {ECO:0000313|EMBL:KKW47755.1};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 371..558
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 187..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388..395
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 713 AA; 76911 MW; 220615DC77EA9F9D CRC64;
MAKKNRSKKK KELSKSRLPS EAAAKEGLHP DIKKSVLAIA FLGLAVIFVL ASFGNAGPAG
SLLYLIFDRL FGIGYYLLPL TSLALAGVFL FSEERRFYGV TLLGAAFFVA AGLGLIDVIG
PERAGWTGSA IGSIETLFGY TASIVILGTL LVASAIVMLN APLRFRWPRQ EDEESTEQEE
MEIAVTLPEA PPVLAEAPNP PKADGGKEEE KSEEASKTPR SAHATARAQS ISQKFKNYVA
PPLSLLKSSV EKPTPGDLRA NANIIKRTLE SFGIPVEMGE INIGPKVTRY TLKPAEGVKL
SRITALNQDL SLALAAHPIR IEAPIPGKSL VGIEVPNKSA AVVRLGSLMA YSEFHSAAST
LTFVLGRDVS GEPIFADITK MPHMLIAGAT GSGKSVAIHS LIVSLLYKNS PETLRLAMID
PKRVELSIYR DIPHLIAPVV TEGKKALSVF RWAISEMERR YELLQHAGAR DIKSYNHGMK
KEPLPYIVIV IDELADLMAA YGRDVEGAVV RLAQMARATG IHLVMSTQRP SVEVITGLIK
ANITARVALQ VASQVDSRTI LDTGGAEKLL GGGDMLFVSS EFSKPKRIQG AYISEEEIHT
VADFIREHNK DISSDEEISF GNGAPGSPGA AAGTNLFENF SPGEDDEDDM YEEAVRVVRE
AQKASASLLQ RRLKLGYARA ARLLDIMEER GIVGPGDGAK PREVFVGNNE EPS
//
