ID A0A255Z873_9PROT Unreviewed; 884 AA.
AC A0A255Z873;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=CHU95_00920 {ECO:0000313|EMBL:OYQ37621.1};
OS Niveispirillum lacus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Niveispirillum.
OX NCBI_TaxID=1981099 {ECO:0000313|EMBL:OYQ37621.1, ECO:0000313|Proteomes:UP000216998};
RN [1] {ECO:0000313|EMBL:OYQ37621.1, ECO:0000313|Proteomes:UP000216998}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TH1-14 {ECO:0000313|Proteomes:UP000216998};
RA Cai H.;
RT "Niveispirillum cyanobacteriorum sp. nov., isolated from cyanobacterial
RT aggregates in a eutrophic lake.";
RL Submitted (JUL-2017) 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:OYQ37621.1}.
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DR EMBL; NOXU01000012; OYQ37621.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A255Z873; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000216998; 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:OYQ37621.1};
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:UP000216998};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 51..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 181..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 510..729
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 527..534
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 884 AA; 94446 MW; 560322A247D5F3ED CRC64;
MPSRSAPQTP PPAGRPAPRG PAPGPGIGAG PGSRRSGLLP EGMLVFALRR LVEGAGLLVM
LLGVALLLSF LSYDSRDPSW STAVPGDTIP VSNLLGRSGA YTADLLLQSL GYAAYLLPLF
LLGWGLRVFR HRPVRNIALR VPLALAAVLV TAMAMVCLAN GNAAWGGPAG ALLVKPLLKL
VVALAGSVSG LMMGLVLLVP AIFLCLWALD VRLWEVGEFI RTLRRRAATL RRATARADAD
EEAVPPPAPV QPTRWAPKPE TAGGSPDMAT LATKAGALLG SLRARIKGTG SAAAPTAVPP
RVAPSLGDPG PGGSTDAAAE PPATERISAP AEERRRHAPP VVGPAPKPLP EVARKVEKAR
QANLLLEPEA RGDYELPPLD ILQLPPHGAG PLMSEEALQR NAEMLESVLE DFGVRGQIVK
VSPGPVVTLY ELEPAPGVKS ARVIGLADDI ARSMSAVSVR VAVVPGRNVI GIEMPNQRRE
TVYLRELLMS DAYEKSQQKL ALVLGKDIGG GPVIADLARM PHLLVAGTTG SGKSVAINTM
ILSLLYRMPP DKCRFIMVDP KMLELSIYEG IPHLLAPVVT DPKKAVVALK WAVREMEDRY
RNMSKLGVRN IDGYNARLKE ARQNAEVLMR RVQTGFDPDT GKPIYEEQPI DLTELPYIVV
IVDEMADLML VAGKDIEAAI QRLAQMARAA GIHLIMATQR PSVDVITGTI KANFPTRISF
QVTSKIDSRT ILGEMGAEQL LGQGDMLYMA GGGRITRVHG PFVRDEEVEQ AVKFLKAQGE
PSYVDAVTEE DEEFDPSAAE SSGGGGGDGG REASGDDLYD QAVAVVTREG KASTSFIQRH
LRIGYNSAAR LIERMEKEGV ISKANHAGKR EVLARNVDDR ESYN
//
