ID D6XU22_BACIE Unreviewed; 810 AA.
AC D6XU22;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Cell division protein FtsK/SpoIIIE {ECO:0000313|EMBL:ADH99308.1};
GN OrderedLocusNames=Bsel_1801 {ECO:0000313|EMBL:ADH99308.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99308.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH99308.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001791; ADH99308.1; -; Genomic_DNA.
DR RefSeq; WP_013172732.1; NC_014219.1.
DR AlphaFoldDB; D6XU22; -.
DR STRING; 439292.Bsel_1801; -.
DR KEGG; bse:Bsel_1801; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_6_9; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000000271; 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 GO; GO:0007059; P:chromosome segregation; 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}; Cell cycle {ECO:0000313|EMBL:ADH99308.1};
KW Cell division {ECO:0000313|EMBL:ADH99308.1};
KW Chromosome partition {ECO:0000256|ARBA:ARBA00022829};
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 459..657
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 236..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 776..810
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..810
FT /note="Basic and 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 810 AA; 88295 MW; A2731CE8EFDC32D7 CRC64;
MSTGKKPASG GKKSPASGKK SVNQPKAEKP GWIRELRFEL SGMFMIVIGI IALFELGLVG
RWIDLFFRFL AGNWKMLFIL TFIGFALYVM IKRQLPPLWN RKLLGYYLLL ISILLISHGR
AYAAWQSQTA PMEGGILGET WGLLTGSPSA AASAADTAGG GMTGALLFSA THALFSTAGT
YVFAGGLMIA AVVFLTGKTF IEILQHEDGP KAWLQAAGRQ TKRSMTSIIK RLKDRKLRKQ
TPDDQAKGTE VEEEPEILDF TERVSGSQSN VVAEIHDETP EAEISEEEHS SDKKPEEETE
QDLETVSDDK AHLVVRESEN KEYLLPPLDL LKSGGKPNQS KEHSMLSKNA RKLEETLESF
GVKAKVTKVH LGPSVTKYEV YPDKGVKVSK IVNLTDDLAL ALAAKDIRME APIPGKSAIG
IEVPNQEVSL VTLREVLDAG LAQDKGNPLS IGLGRDISGS AILAELNKMP HLLVAGATGS
GKSVCINGII VSILLRAKPH EVKMMMIDPK MVELNVYNGI PHLLAPVVTE PKKAAQALKK
VVSEMERRYE LFAASGTRNL EGYNDYIRKE NMKRDEAEAY APLPYIVVIV DELADLMMVA
SSEVEDAITR LAQMARAAGI HLIIATQRPS VDVITGVIKA NIPSRIAFGV SSSTDSRTIL
DGNGAEKLLG KGDMLFVPVG ASKPTRIQGA FLSDDEVERI VSHCIEQQKA QYAEEMIPAE
VEDKKPTGEA EDDLYPDAVA LVTDMQSASV SMLQRRFRVG YARAARLIDE MEVRGVVGPY
EGSKPREVLV SKPSEESEHS SDHGINGTKE
//
