ID A0A1D7NIG3_9SPHN Unreviewed; 803 AA.
AC A0A1D7NIG3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=BG023_11617 {ECO:0000313|EMBL:AOL93570.1};
OS Porphyrobacter sp. LM 6.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Porphyrobacter.
OX NCBI_TaxID=1896196 {ECO:0000313|EMBL:AOL93570.1, ECO:0000313|Proteomes:UP000094080};
RN [1] {ECO:0000313|EMBL:AOL93570.1, ECO:0000313|Proteomes:UP000094080}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM 6 {ECO:0000313|EMBL:AOL93570.1,
RC ECO:0000313|Proteomes:UP000094080};
RA Hentchel K., Vargas G., Fiebig A., Coleman M., Crosson S.;
RT "Genome sequences of bacteria isolated from the littoral zone of southern
RT Lake Michigan.";
RL Submitted (AUG-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; CP017113; AOL93570.1; -; Genomic_DNA.
DR RefSeq; WP_069309159.1; NZ_CP017113.1.
DR AlphaFoldDB; A0A1D7NIG3; -.
DR STRING; 1896196.BG023_11617; -.
DR KEGG; porl:BG023_11617; -.
DR PATRIC; fig|1896196.3.peg.621; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000094080; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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; 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; 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 30..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 180..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 438..657
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 238..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 455..462
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 803 AA; 86464 MW; 6C277E21E5FEDD9F CRC64;
MASRAVNPVK PGRKTDAEWR AGLRRGMRRL AQMTGAGLLF GAAVFLALAL ASYTQTDPSP
STAADPAEVA NWMGASGAWV ADRVLLIFGL PGVLLLPLLY VSARKLWRDV ENGDEPETTP
WWLPTGLLLI AMTLIATVLS LSFSGPGGTL PAQAGGLAGL LGAGAVEAVA ARFGAEAEGW
VILGLALTSL AVAVGLLTRI FAIDWRVLLS LPDFLGGGTL AGLLRRLPLP GRKRAAASPL
AFADDDEDEP APRARRAAKG AAVTTEIDDR PRRAPEISDP SAPPKRAAVP AKVAQGDMFA
AFKLPSLDLL AEPPVDKAPK LDKMALERNA RLLENVLDDF NVKGEITAVR TGPVVTMYEL
EPAPGIKASR VVGLAEDIAR NMSAISARVS PIPGRTVMGI ELPNQDRQTV MLKELAAAAA
FVDAKGNLPI ILGKDIAGEP IIADLAAMPH LLVAGTTGSG KSVGLNVILL SLLYRFTPAE
LRLILIDPKV LELKTYDDIP HLLSPVVTEP HKSVRALKWA VEEMERRYRM MSAISSRNIN
SFNEKVSAAI AKGKPLGRRV QTGFDPETGE QLFEEEQLDY APLPQIVLIV DELADLMVTV
GKEIEVLIQR LSQKSRAAGI HLIMATQRPS VDVITGVIKA NLPTRISFKV TSRIDSRTIL
GEQGAEQLLG KGDMLYKPNT GAMVRVHGPF VSDEEVEAVA TFWRGQGAPE YVDAVTEEPE
DGGFGFEDDF TASDNPEERK YRQACQIVIE NQKASGSWLQ RQMGVGYNTA AKWIERMEED
GLVGPANHVG RREIYRDRDG NPL
//
