ID A0A126ZFT2_9BURK Unreviewed; 796 AA.
AC A0A126ZFT2;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:AMM25454.1};
GN ORFNames=AX767_14615 {ECO:0000313|EMBL:AMM25454.1};
OS Variovorax sp. PAMC 28711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM25454.1, ECO:0000313|Proteomes:UP000070169};
RN [1] {ECO:0000313|EMBL:AMM25454.1, ECO:0000313|Proteomes:UP000070169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM25454.1,
RC ECO:0000313|Proteomes:UP000070169};
RA Park H.;
RT "Complete genome of Variovorax sp.";
RL Submitted (FEB-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; CP014517; AMM25454.1; -; Genomic_DNA.
DR RefSeq; WP_068632001.1; NZ_CP014517.1.
DR AlphaFoldDB; A0A126ZFT2; -.
DR STRING; 1795631.AX767_14615; -.
DR KEGG; vaa:AX767_14615; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000070169; Chromosome.
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, ECO:0000313|EMBL:AMM25454.1};
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:UP000070169};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..106
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 248..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..266
FT /note="Basic and acidic residues"
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 796 AA; 87064 MW; F53D2C866B9B44D9 CRC64;
MTYSLNTLQS SSADGQPVRQ RAMRFAHEIT LIAGFVVLLF WLLAMLSFTP SDAAWSTSGT
GGEVKNWAGR LGAWLADGSY FLAGYSVWWC LAAGLRVWLS SLAGWLRGGE VAPAEEPVRG
RFNRSRLAFW CGLVLLLCAS AMLEWSRLYR LEFRLPGHGG GVLGYFVGPM SVKWMGFTGS
ALIAIAGGVI GSALVFRFSW SQIAERIGSR VYSLFESRRE KREIAADIAL GKQAVRERAA
AEDMPLMRND SEVESADEEL RIDPPAKPRR APSPPVQIEP AMTEVPRSER VVKERQKPLF
KELPDSKLPQ VDLLDAAQVR QETVSADTLE MTSRMIEKKL KDFGVEVRVV LASPGPVITR
YEIEPATGVK GSQILGLAKD LARSLSLVSI RVVETIPGKN YMALELPNAK RQSIKLSEIL
GSQIYNEGKS MLTMGLGKDI IGNPVVADLA KMPHVLVAGT TGSGKSVGIN AMILSLLYKA
EARDVRLLMI DPKMLEMSVY EGIPHLLAPV VTDMRQAAHG LTWCVAEMER RYKLMSKLGV
RNLAGYNTKI DEAKAREEFI YNPFSLTPDD PEPLKREPHI VVVIDELADL MMVVGKKIEE
LIARLAQKAR AAGIHLILAT QRPSVDVITG LIKANIPTRI AFQVSSKIDS RTILDQMGAE
ALLGMGDMLY MPSGTGLPIR VHGAFVSDEE VHRVVAYLKS QGAPDYIEGV LEGGTVDGDG
DLMGDGGGDA EKDPMYDQAV EVVLKNRKAS ISLVQRHLKI GYNRAARLVE DMEKAGLVSS
MSGSGQREIL VPARAE
//
