ID A0A0X3U079_9RHOB Unreviewed; 964 AA.
AC A0A0X3U079;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=AVO44_11660 {ECO:0000313|EMBL:KUJ79030.1};
OS Ruegeria profundi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Ruegeria.
OX NCBI_TaxID=1685378 {ECO:0000313|EMBL:KUJ79030.1, ECO:0000313|Proteomes:UP000053690};
RN [1] {ECO:0000313|Proteomes:UP000053690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZGT108 {ECO:0000313|Proteomes:UP000053690};
RA Zhang G., Stingl U.;
RL Submitted (DEC-2015) 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}.
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:KUJ79030.1}.
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DR EMBL; LQBP01000005; KUJ79030.1; -; Genomic_DNA.
DR RefSeq; WP_068337082.1; NZ_LQBP01000005.1.
DR AlphaFoldDB; A0A0X3U079; -.
DR STRING; 1685378.AVO44_11660; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000053690; 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, ECO:0000313|EMBL:KUJ79030.1};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 598..817
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 297..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 358..379
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 615..622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 964 AA; 104701 MW; 0303AA48B4008D5C CRC64;
MASYNARKRD PLLDSTTQAA IERRSKELIG IALILLGLAS AAMIWSYTPD DPNWMVSTDA
PVQNWMGRIG ASIAAPLFMI VGWGSWGIAL VLIGWGARFT GHFGEDRAVN CLIFAPIWIA
VVSVYAATLV PGEAWRATHS YGLGGLFGDT VMGALLTLLP LSSHFMVKLM SLAMAVGMLA
LGVFVLGFTK SDVRKGFRAF LLGLVMSYDM LMNVMGRGAA ATAQAARDRR AQWDERKAAR
AEAAEAVFDD DVAFADPVFE DLEYAEPEPA KSGLLARMPS LIRRPDPMPE PELIDQDPVA
GFDEMPGEDR IRSKISAAVR NRKVATGEMT PEPDPNLPLT KGRGRGPDPL ILNPRGTGEL
PPEPPVTSAG LPPEPMQTAT PDPEWQDTLH DDFAPEPYDQ DDDVFEDAPE PEPQPRPAMK
IPVAEPRKPV VAQPVRRTPP PSRRAQAEAQ PALSFEERHS DFELPPLGLL SNPASIQRHH
LSDEALEENA RMLENVLDDY GVKGEIVSVR PGPVVTMYEL EPAPGLKASR VIGLADDIAR
SMSALSARVS TLPGRSVIGI ELPNENREMV VLREILASRD FGDGNQALPL ALGKDIGGES
VVANLAKMPH LLIAGTTGSG KSVAINTMIL SLLYKLTPDE CRLIMIDPKM LELSVYDGIP
HLLSPVVTDP KKAVVALKWV VGEMEDRYRK MSKMGVRNIA GYNGRVKDAL AKGEMFSRTV
QTGFDEETGE PMFETEEFAP EAMPYIVVIV DEMADLMMVA GKEIEACIQR LAQMARASGI
HLIMATQRPS VDVITGTIKA NFPTRISFQV TSKVDSRTIL GEMGAEQLLG QGDMLYMAGG
AKITRCHGPF VSDEEVEEIV NHLKQFGPPD YVGGVVDGPA EEKADNIDAV LGLNTGGNTN
GEDALYDQAV AIVIKDRKCS TSYIQRKLAI GYNKAARLVE QMEDEGVVSS ANHVGKREIL
VPEQ
//
