ID A0A1G1CCL0_9BACT Unreviewed; 835 AA.
AC A0A1G1CCL0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=A3K19_01490 {ECO:0000313|EMBL:OGV92814.1};
OS Lentisphaerae bacterium RIFOXYB12_FULL_65_16.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798581 {ECO:0000313|EMBL:OGV92814.1, ECO:0000313|Proteomes:UP000179250};
RN [1] {ECO:0000313|EMBL:OGV92814.1, ECO:0000313|Proteomes:UP000179250}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGV92814.1}.
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DR EMBL; MHBP01000073; OGV92814.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1CCL0; -.
DR Proteomes; UP000179250; 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};
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 41..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..203
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 459..659
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 251..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 803..835
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..294
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..835
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 476..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 835 AA; 89209 MW; FEA059CE9EF5D0ED CRC64;
MAGTAGTLCV AKGALVNVNG KRPAMTTAGE QDGQKRGVRH VVFFVLGLLV FLSLVSYDPA
DADYLAGGLG EPGVIRNWIG YFGAWVSRLL LLTFGFAAYA FAALVLLASS RRLFGRQGLR
RIAWDYWVAM MLVAVGLAML LGIWPNVGAV VASALNIGGI PGGVFGQRFC APDGGWIRVI
LNPTGSAIVA LALVVVGLVV VWVHDWQDLA LEQLGPTGAA DSGAQAEAGE GGAGKLGRWA
QRRIARLRER ELLQDEAELE PPPKKAPRKE PPEEPVADAL PLPVQEPPPP TAPVAPVAPA
APVKPAVVPA RTKATAPPQP PKYKLPSLDV LHPDDGVTTT VDEKEVARKK EILQATLDSF
QIEAQVGEAT SGPRVTLFEV LPAPGVKVER ISQISNNIAM ELRAVSLRIL TPIPGKNTVG
IEVPNLKAAT VGLRSLMASP EWTNSKAKIP VLLGRNISGQ VVILDLTKAP HLLIAGATGS
GKSVCINVVI MSLLYRFTPE ELRLIMVDPK VVEFRAYEKL PHLVVPVISD SKKVPLALRW
VIHEMGWRYQ VLAKVGARNL EGFNARKKSP TPVMDEGGNP IPDRLPFIVV IIDELADIMM
TAKADVETSL ARIAQLSRAV GIHTIIATQR PSVNVLTGVI KANFPTRIAF QVTSQTDSRV
IMDGKGAEAL LGRGDMLFKP PGASRLERNQ GAMVDDDEID LVVKACADQR EQQFDENVFK
LAAAGGPAAE EAGAGAPLTE EDEQLVQQAI EIIVRDRKAT TSYLQRRMGI GYNRAASMME
LLEERGVIGP QVGTAPREIL VLGKEGEGAT DPDAVDASDA DEGSDSDGDA EDGER
//
