ID A0A0G0MWM0_9BACT Unreviewed; 736 AA.
AC A0A0G0MWM0;
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=Translocase FtsK protein {ECO:0000313|EMBL:KKQ78074.1};
GN ORFNames=UT00_C0002G0072 {ECO:0000313|EMBL:KKQ78074.1};
OS Parcubacteria group bacterium GW2011_GWA1_38_7.
OC Bacteria.
OX NCBI_TaxID=1618783 {ECO:0000313|EMBL:KKQ78074.1, ECO:0000313|Proteomes:UP000034610};
RN [1] {ECO:0000313|EMBL:KKQ78074.1, ECO:0000313|Proteomes:UP000034610}
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:KKQ78074.1}.
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DR EMBL; LBVD01000002; KKQ78074.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0MWM0; -.
DR PATRIC; fig|1618783.3.peg.215; -.
DR Proteomes; UP000034610; 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};
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 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 66..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 370..577
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 710..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387..394
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 736 AA; 80830 MW; 83243FE55EF0CEC8 CRC64;
MAKKNNKKED RKDTDFGLKK LKDETISWIL AIIFFMLSIF FVLASFHKAG FVGTKVFDIF
SKLFGYGYYL LPTVFFILGI SFTNSIKRSF GATKFIGASL FFVSSLALLD FTFAQFGFIK
KGGFVGNILQ GPLVKLFDVY ATPAMLISLI FISVLVIFDA TINISSILNI FRKKKEGESD
ETEEKAVKIL NSNEKTEEGY QGKIAPQITQ GVDKRSLQTE GGDDFGVRKN IISFKPFPPP
PLSLLERDRG KPEVGDIKAN SNIIKRTLQN FGIIVEMDEI SIGPSVTRYA LKPAEGVKLS
KILGLQNNLE LALAAHPVRI EAPIPGKSLV GIEIPNSVKT MVGLGSILSQ SGYTDSEKSL
TIALGKSISG ASIFANIAKM PHLLIAGATG SGKSVTIHVL INSLLFRNSA ENLKFIMIDP
KRVELTQYNK IPHLLTPVIT DAKKVIMSLK WASKEMDRRY DILETNKVRD IESYHKNILS
PALEKFKKNP PAGAGGGEVP ELMPYIVIVI DELADIMQAY PRELESAIIR LAQMSRAVGI
HLILSTQRPS VNVITGLIKA NIPARIALQV ASQFDSRTIL DTAGAEKLLG AGDMLYISGE
MSKPIRLQSP FISENEVKKV VEYLVKNAED EIPTSIDMEA DKSKNIVFES LVGGGESEDD
LYEEAREIVI GAGKASTSYL QRKLRIGYAR AARLMDILEE NGVVGGGDGA KPRDVLIKPE
GGFATDQNEE QENEHL
//
