ID A0A1I4UBM4_9BURK Unreviewed; 797 AA.
AC A0A1I4UBM4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SFM86231.1};
GN ORFNames=SAMN05444747_11027 {ECO:0000313|EMBL:SFM86231.1};
OS Variovorax sp. OV329.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1882825 {ECO:0000313|EMBL:SFM86231.1, ECO:0000313|Proteomes:UP000199688};
RN [1] {ECO:0000313|EMBL:SFM86231.1, ECO:0000313|Proteomes:UP000199688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV329 {ECO:0000313|EMBL:SFM86231.1,
RC ECO:0000313|Proteomes:UP000199688};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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. Translocation stops specifically at Xer-dif sites, where FtsK
CC interacts with the Xer recombinase, allowing activation of chromosome
CC unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC the direction of DNA translocation. FtsK can remove proteins from DNA
CC as it translocates, but translocation stops specifically at XerCD-dif
CC site, thereby preventing removal of XerC and XerD from dif.
CC {ECO:0000256|ARBA:ARBA00024784}.
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}.
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DR EMBL; FOUG01000010; SFM86231.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4UBM4; -.
DR STRING; 1882825.SAMN05444747_11027; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000199688; 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 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199688};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 127..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 442..651
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 239..276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 459..466
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 797 AA; 87108 MW; A799B1D20DFA5D74 CRC64;
MTYSLNTLQS AAGAGSPPAR TRALRFAHEL TLIASFVLLL FWLLAMLSYT PSDSAWSTSG
TGGEVKNWAG RLGAWLADGS YYLAGYSVWW CVAASWRAWM SSLAGWLRGV EGGQAEAPKG
RFNRSRIAFW FGLILLLCAS AMLEWSRLYR LEFRLPGHGG GVLGYLVGPL SVKWLGFTGS
ALVAIAGGVI GSALVFRFSW TQIAERIGSR LYSLFESRRE KREIAQDIAM GKKAVRERER
EESILGGDRD MDDVEGPDEE LRIEPRPKRR PPAPPVQIEP ALAEVPKSER VVKERQKPLF
KELPDSKLPQ VDLLDAAQAR QETVSSDTLE MTSHLIEKKL KDFGVEVRVV LASPGPVITR
YEIEPATGVK GSQIVNLAKD LARSLSLVSV RVIETIPGKN YMALELPNAK RQSIKLSEIL
GSQVYNEAKS MLTMGLGKDI VGNPVVADLA KMPHVLVAGT TGSGKSVGIN AMILSLLYKA
EANDVRVLMI DPKMLEMSVY EGIPHLLAPV VTDMKQAAYG LNWCVGEMER RYKIMSKVGV
RNLAGYNAKI DEAKSRGEFI YNPFSLTPDD PEPLKREPHI VVVIDELADL MMVVGKKIEE
LIARLAQKAR AAGIHLILAT QRPSVDVITG LIKANIPTRI AFQVSSKIDS RTILDQMGAE
ALLGMGDMLY MASGTGLPVR VHGAFVSDEE VHRVVAYLKS QGEPDYIEGV LEGGTVDGEG
DLLGEGGAEG GEKDPMYDQA VEVVLKHRKA SISLVQRHLK IGYNRAARLV EDMEHAGLVS
AMSGSGQREI LVPARSE
//
