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Database: UniProt
Entry: A0A0G0KQG1_9BACT
LinkDB: A0A0G0KQG1_9BACT
Original site: A0A0G0KQG1_9BACT 
ID   A0A0G0KQG1_9BACT        Unreviewed;       785 AA.
AC   A0A0G0KQG1;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Cell division FtsK/SpoIIIE {ECO:0000313|EMBL:KKQ51354.1};
GN   ORFNames=US70_C0018G0006 {ECO:0000313|EMBL:KKQ51354.1};
OS   Parcubacteria group bacterium GW2011_GWD2_38_11.
OC   Bacteria.
OX   NCBI_TaxID=1618941 {ECO:0000313|EMBL:KKQ51354.1, ECO:0000313|Proteomes:UP000034843};
RN   [1] {ECO:0000313|EMBL:KKQ51354.1, ECO:0000313|Proteomes:UP000034843}
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   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC       {ECO:0000256|ARBA:ARBA00025923}.
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:KKQ51354.1}.
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DR   EMBL; LBTZ01000018; KKQ51354.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0KQG1; -.
DR   STRING; 1618941.US70_C0018G0006; -.
DR   PATRIC; fig|1618941.3.peg.662; -.
DR   Proteomes; UP000034843; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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; 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; SM00382; AAA; 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:KKQ51354.1};
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        27..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        99..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        138..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          400..606
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          186..211
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        191..209
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         417..424
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   785 AA;  86752 MW;  40E0090C55AE0FA1 CRC64;
     MGRRKKQQEE VENEQPKPII HGDAKRSLVA IFLFALAILF VLGFLADAKI VGTGWLLSML
     NSIVGWMFGV GKYISPIVLI IAGIILLFRK ETLFYVSKLI GLSIAFASIL GLIHILAYDA
     GEMLKVAKLG EGGGFLGYIS AIILLKLTGI VGGSVILVAT LLMGAIVAFN FSLVNVVRRF
     FHKKNTQENA EEEEETEEES EEETEEILEN PIIEVEKEEN IKQTEFVQDP NEQDEMDSRM
     DKVLKKAAAW MPKGKDRAKK EQLELAWDLP PVDLLDSAIE KAQGGDVQKN AKIIQETLHN
     FGIEVELGEI KTGPTVTQYS FRPAVGVKLS RITTLSSDLA LRLAARQVRI EAPIPGKSLV
     GIEVPNKTNA TIRLPELLSA LEFENRKSNL LLALGKDVSG NYIFGDLKKM PHLLIAGSTG
     SGKSVCINTI LLSMLYQNSP DELKLILVDP KRVELTPYNG IPHLLTDVIV ENGKVLSALK
     WAIGEMERRY KLLQGVGSKD IASFNKKAES GEMLKKVNTD TGEITEESFE KIPFIVIVID
     ELADLMASHG KEVEGAIIRL AQMARAVGIH LILSTQKPIV TVITSLIKSN IPTRIAFRVP
     SLMDSRTILD ASGAEKLLGN GDMLFSAAEA VDLRRVQGVF VSEEEVKRVV EFIKKQKFEK
     IEDDLGEEIV ASETKPEGNH NGEVKTLQYA DKIDFDSIEA NENEDSLYDE AKKIVIQSGK
     ASSSLLQRRL RIGYSRAARL IDILEDRGIV GEADGAKPRE ILVANDQPAY QDTMTDQVAR
     DKWQM
//
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