ID A0A1G9BFG8_9PROT Unreviewed; 778 AA.
AC A0A1G9BFG8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SDK38193.1};
GN ORFNames=SAMN05192566_1147 {ECO:0000313|EMBL:SDK38193.1};
OS Methylophilus rhizosphaerae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylophilus.
OX NCBI_TaxID=492660 {ECO:0000313|EMBL:SDK38193.1, ECO:0000313|Proteomes:UP000198629};
RN [1] {ECO:0000313|EMBL:SDK38193.1, ECO:0000313|Proteomes:UP000198629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBMB127 {ECO:0000313|EMBL:SDK38193.1,
RC ECO:0000313|Proteomes:UP000198629};
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; FNFX01000002; SDK38193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9BFG8; -.
DR STRING; 492660.SAMN05192566_1147; -.
DR Proteomes; UP000198629; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 421..630
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 692..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 438..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 778 AA; 85507 MW; E62D04792F0C95A6 CRC64;
MRKERDNALF FNKKSISNAR LERESTEKQL KDAKLVREVT WIALAALGVF LAVILVSYSH
EDPGWTHAIG ENGIVHNAGG VVGAWIADVL LSLFGFSSWW FVILAFYFVW LMYQRLHLDA
AEKQDWWLNG VGFALLLLAS AALESGHLVN FPADFPLKQG GVIGSGIDHL LRNMFGFAGS
TMLLLVLFAT AFSLFTGWSL ISMSEQLGEG VIRLYQWSLL KYQDFQDRQV GRQVLQAREE
FVEAERKRIE DRKPVEITVP EIVIEPSERV VKEKQAVLFE VITQEGLPPL HLLDAPNQSV
ELQSAETLDF TSRLIERKLM DFGIEVKVVT AQPGPVITRY ELDPAPGVKG SQITNLAKDL
ARALSVISVR VVETIPGKSY MGLEIPNPKR QIVSLSEIMG SQAYADLNSP LAIAMGKDIA
GKPIVADLAK MPHVLVAGTT GSGKSVAINA LILSLLYKSE ASRVRMILID PKMLELSVYE
GIPHLLAPVV TDMRQAANAL NWCVAEMERR YKLMSTLGVR NLAGYNQKIQ EAKKQGTPIP
HPFSLTPDEP EPLDEMPLIV VVIDELADLM MVVGKKVEEL IARLAQKARA SGIHLVLATQ
RPSVDVITGL IKANVPTRVA FQVSSKIDSR TILDQMGAET LLGQGDMLYL PPGSGYPQRI
HGAFVSDGEV HNVVNFLKAQ GEPNYIEGIL TNETEGGDLD GMSGGEDGGG EKDPLYDEAV
AIVLKTRRAS ISSVQRQLRI GYNRAARLIE DMERAGLVSA MQSNGNREVL VKAGGEHE
//
