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Database: UniProt
Entry: A0A0K8PAT8_9CHLR
LinkDB: A0A0K8PAT8_9CHLR
Original site: A0A0K8PAT8_9CHLR 
ID   A0A0K8PAT8_9CHLR        Unreviewed;       854 AA.
AC   A0A0K8PAT8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE {ECO:0000313|EMBL:GAP39772.1};
GN   ORFNames=ATC1_12307 {ECO:0000313|EMBL:GAP39772.1};
OS   Flexilinea flocculi.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Flexilinea.
OX   NCBI_TaxID=1678840 {ECO:0000313|EMBL:GAP39772.1};
RN   [1] {ECO:0000313|EMBL:GAP39772.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TC1 {ECO:0000313|EMBL:GAP39772.1};
RA   Matsuura N., Tourlousse D.M., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA   Cruz R., Yamaguchi T., Sekiguchi Y.;
RT   "Draft Genome Sequence of Anaerolineae Strain TC1, a Novel Isolate from a
RT   Methanogenic Wastewater Treatment System.";
RL   Genome Announc. 3:e01104-15(2015).
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
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DR   EMBL; DF968180; GAP39772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K8PAT8; -.
DR   STRING; 1678840.ATC1_12307; -.
DR   PATRIC; fig|1678840.3.peg.869; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000053370; 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   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; IPR003593; AAA+_ATPase.
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; 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}; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053370};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        45..71
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        91..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        125..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        156..175
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          497..685
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          250..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        256..270
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         515..522
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   854 AA;  95798 MW;  D1CB4B2241E48103 CRC64;
     MTSIQPKKKV KASYRGDKKP SMAARKKAAT IAAKRNKKAL SNTPLSFYSI FSIFADFIGL
     LLLLSGILIF FSLKFPEMIS LTEWCSRFIL FYAGKSAYFS GGIFVLAGLW ILILRRIKKP
     FSFSWKFFIF FIVVYQYILV LIQHEENADA YVYGKFANLA GGVVAGQIDA ALFTAVGNAG
     SILIYCFSAL IMLLIAWLWI SNSFSNSLHI HPAFFSPLRK KLKSLFRNLS RSNAVYITEP
     DPKKEAIPFN FSDTEPPLEE VKDQKKPSVT RSKKSRTAAN EVTENVISDD RIAKPDSKTD
     LEKTFHTQKK IDPLPEKIQP VTFLKNSFRP SLSERLGKQE TTEKKDELVI SWRLPITDEI
     LDPIKIRQNI TSEDPHIQGQ IQKIEHVLDA FDAPGKVVDI QIGPTFTQYG IEPGFMERAD
     RKTRVRVKQI ENVKKDLEMA LSVKQLTIEA PIPNKTFIGL QVQNKYRIPV TLREIIESDV
     FQKNRKGLGI ALGKDINGAV YAADLTRMPH LLIAGATGSG KSVCLNAILV CLLMNYTPDQ
     LKLVLIDPKR VELTGYNGIP HLITPVITDV EQVGNVLQWI LREMDMRNLH FMQTGVRNIQ
     DYNQKNPDKI LPYLVVVIDE LANLMMEAAS DIETSITRLA QTARAMGIHI IVATQRPSRD
     VITGTIKGNL PSRIAFAVAT NIDSHVILDR SGAENLFGKG DMYFMSSEDS NLKRLQCVYV
     SDDEIRKLVD YWKKNPRIGD EQSEMKTNTI SLVTVRAQPQ ITQGTLTQLP MLNEDISSVK
     KGDDPLLNEA IAMVRKQGRA SANMLVSRLS IGFTRANKLL SQMEDMGIIS PPNANPAIPR
     EILDYGENGA PPED
//
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