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Entry: A0A098YBN4_9ACTN
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ID   A0A098YBN4_9ACTN        Unreviewed;       838 AA.
AC   A0A098YBN4;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KGH47899.1};
GN   ORFNames=IN07_05140 {ECO:0000313|EMBL:KGH47899.1};
OS   Modestobacter caceresii.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=1522368 {ECO:0000313|EMBL:KGH47899.1, ECO:0000313|Proteomes:UP000029713};
RN   [1] {ECO:0000313|EMBL:KGH47899.1, ECO:0000313|Proteomes:UP000029713}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KNN45-2b {ECO:0000313|EMBL:KGH47899.1,
RC   ECO:0000313|Proteomes:UP000029713};
RA   Bukarasam K., Bull A., Girard G., van Wezel G., Goodfellow M.;
RT   "Biosystematic studies on Modestobacter strains isolated from extreme
RT   hyper-arid desert soil and from historic building.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Essential cell division protein that coordinates cell
CC       division and chromosome segregation. The N-terminus is involved in
CC       assembly of the cell-division machinery. The C-terminus functions as a
CC       DNA motor that moves dsDNA in an ATP-dependent manner towards the dif
CC       recombination site, which is located within the replication terminus
CC       region. Required for activation of the Xer recombinase, allowing
CC       activation of chromosome unlinking by recombination.
CC       {ECO:0000256|ARBA:ARBA00024986}.
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:KGH47899.1}.
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DR   EMBL; JPMX01000015; KGH47899.1; -; Genomic_DNA.
DR   RefSeq; WP_036334044.1; NZ_JPMX01000015.1.
DR   AlphaFoldDB; A0A098YBN4; -.
DR   STRING; 1522368.IN07_05140; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000029713; 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, ECO:0000313|EMBL:KGH47899.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000029713};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        97..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        130..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        163..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        212..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          486..686
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          251..287
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..285
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         503..510
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   838 AA;  89293 MW;  94A82051FEE60276 CRC64;
     MPARASTSNR APARGSAPAR PRSGSTAAKK RPPAKRGSTA ARRPPPKKKQ GTLAGSLWRC
     ASGAWGLLAR SAGGVARSVA RPEEAEPLGP EHRRDGVGLA VLGLAIVLGA AVWTDGIGPV
     GAGLATGVEW TIGALTVALP VVLLLVALRL LRHPPHPESR GRLMIGWLSV IAAVVGVAHV
     VGPDADPADR TGAGGLLGWA VGMPLTAGVG PIVTVLLLVL LAFFGVLVVT ATPVHQVPER
     LREWADRQLG RDGDEEYGDY DEYQDEEPAT EPVPRVRKGR KAAAPAVEDT LDTGSIDLGA
     LDEAPEAVVH EPAPEPVPVR RPAIIDRTAP PEDLPPIEEP EQLRIQPVEG AYTLPSVSVL
     RAGTPPRAKS KANDVAIEAI TGVLEQFNID AAVTSFTRGP TVTRYEIELG NAVKVEKITA
     LTKNLAYAVA NDNIRILAPI PGKSAVGVEV PNTDRETVSL GDVMRSQVAK QDPHPMLVGL
     GKDIEGGFVC ANLAKMPHLL VAGATGAGKS SCINSLLTSL LLRATPEQLR MILIDPKMVE
     LTPYDGIPHL ITPIITDPKK AATALAWLVE EMEQRYQDMR ATGVRHIDDF NKKVERGEIT
     APPGSERVYQ PYPYILTIVD ELADLMMVAP RDVEESIVRI TQKARAAGIH LVLATQRPSV
     DVVTGLIKAN VPSRLAFSTS SLTDSRVILD QPGAEKLIGM GDALFLPIGA GKPIRVQGAY
     VSDTEIEAVV EFTKRQAEPE YREEVFTAAA GEKKEIDEDI GSDLELLVQA VELVVTSQFG
     STSMLQRKLR VGFAKAGRLM DLMESRGIVG PSEGSKARDV LIKPDELESV MFTLRGSQ
//
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