ID F2NLJ9_MARHT Unreviewed; 944 AA.
AC F2NLJ9;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Cell division protein FtsK/SpoIIIE {ECO:0000313|EMBL:AEB12098.1};
GN OrderedLocusNames=Marky_1363 {ECO:0000313|EMBL:AEB12098.1};
OS Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Marinithermus.
OX NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB12098.1, ECO:0000313|Proteomes:UP000007030};
RN [1] {ECO:0000313|EMBL:AEB12098.1, ECO:0000313|Proteomes:UP000007030}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX PubMed=22675595; DOI=10.4056/sigs.2435521;
RA Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA Land M., Pan C., Brambilla E.M., Rohde M., Tindall B.J., Sikorski J.,
RA Goker M., Detter J.C., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT chimney.";
RL Stand. Genomic Sci. 6:21-30(2012).
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; CP002630; AEB12098.1; -; Genomic_DNA.
DR AlphaFoldDB; F2NLJ9; -.
DR STRING; 869210.Marky_1363; -.
DR KEGG; mhd:Marky_1363; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_3_1_0; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000007030; Chromosome.
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; 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}; Cell cycle {ECO:0000313|EMBL:AEB12098.1};
KW Cell division {ECO:0000313|EMBL:AEB12098.1};
KW Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000007030};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 598..789
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 402..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 191..218
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 298..350
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 406..441
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..465
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 616..623
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 944 AA; 102588 MW; 00AC96C59F9CA644 CRC64;
MHTSAHRIAL PRWYNAPVGK PKSKRNASVS RGDLEALALV LFGTAFFLGV SVYPDPPLSG
QVGAYLKAAL WGNLGLLSWL FPIPFALAGT LILLKRPLRG LLRESLLTGL AGVSSLPLIA
GVAPEWGGAL GTWAHQALTT RLGPAGLLLA VLALSVVLDL ALRHPPFTLV LTGFKRGIGA
GLNLFRAYRA YRTARAQRAR LRKAASSLAQ EVQALLARYP DHRALATLQA DLKAFLKNPD
AFEPSELEGF RRLLDEFTEA RAAELAERLA AENPGFSSRI QAWLGALNAP LSAHTPLMER
LEERRKALIL EFKAIQEKET RLARRAERAA EALRRSAAGL EAEWKAHEAR LGEWRALEGL
LEDLEARAES WTRWVEWAEQ VGAERHAEAL ERLLEHGLEA APPEAEEAAP PSPADPPAEA
TPPEPPVEEA TAPPPSPNPA PRVSGGSGKT GSVSVHPTTT LSLPSPELLD PPEPKPANAR
DLQADAKQRA EIINETLSHF GLEARVVDWA RGPTVTRFEV EPAPGEKISR IANLANDLAR
ALAVGSVRVE APIPGKSVIG LEVPNAEREL VRFSEALHHP AFQRSRDKLP LILGKSIDGE
MWVRDLAKMP HLLIAGSTGS GKSVCINTLL MSLLYRYLPT ELRFLMIDPK MVELTPYDGI
PHLVRGVVTN PADAAGVLLG AVAHMERRYK MMSQVGARNL EQFNAKMREL GEPTLPYLVI
VIDELADLMI TSPKEVEQAI LRLAQMARAT GMHLILATQR PSVDILTSLI KVNIPARIAF
AVSSSHDSRT ILDTTGAERL TGQGDMLFHQ PGLAKPVRLQ GPFLSDKEIH RITNYLRGQA
FDDAFGEAYG ADFDGPVQLG DPTGGKAGEL DFSDPLLKKA AEIVVEEGQA SVSRLQRRLS
VGHARAGKLM DLLEAMGIVG PHQGSKPREV LITKEELPEY FGEP
//