ID A0A075ML89_9PROT Unreviewed; 752 AA.
AC A0A075ML89;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=I862_06630 {ECO:0000313|EMBL:AIF81880.1};
OS endosymbiont of Acanthamoeba sp. UWC8.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Holosporales; Holosporaceae.
OX NCBI_TaxID=86106 {ECO:0000313|EMBL:AIF81880.1, ECO:0000313|Proteomes:UP000028183};
RN [1] {ECO:0000313|EMBL:AIF81880.1, ECO:0000313|Proteomes:UP000028183}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UWC8 {ECO:0000313|EMBL:AIF81880.1};
RX PubMed=25103769;
RA Wang Z., Wu M.;
RT "Complete Genome Sequence of the Endosymbiont of Acanthamoeba Strain UWC8,
RT an Amoeba Endosymbiont Belonging to the 'Candidatus Midichloriaceae' Family
RT in Rickettsiales.";
RL Genome Announc. 2:e00791-e00714(2014).
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; CP004403; AIF81880.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A075ML89; -.
DR STRING; 86106.I862_06630; -.
DR KEGG; eaa:I862_06630; -.
DR PATRIC; fig|86106.3.peg.1372; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_5; -.
DR Proteomes; UP000028183; 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 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}; Reference proteome {ECO:0000313|Proteomes:UP000028183};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 56..82
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 395..614
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 412..419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 752 AA; 83345 MW; 69526204E2CD9AB1 CRC64;
MIVSKAKFNL NSFFLRCLGA LIIALAIFLF ISFISFNAGD PSFNQVNDNE VKNLAGYYGA
FIADPILQSL GFASYFIVIF LTTLGLKILT LKEIGFLTVR IAFLILLLPF LAACLTFIKP
IPSQNFISYG GFIGVFVKEE LSVYFNPKHI FYSIFPIIII VSLLTLNINY KEFKKFIIVI
IRLFTYGAKL FAWAMVSLYI LIRGKIAKKT NETTVENQEA NIEIEKPKPI LTIKNKMPRF
EPKKDVLYST PRSSSSDFQL PPTALLKEPP ITSKKNQLSE AALNQNSRLL TQVLQDFGVY
GNILSIRPGP VVTLYELEPS AGTKSSRVIG LADDISRSMS AVSARISVIP GKNALGIELP
NTSREIVYLR ELMESETYVA TEGKLPLVLG KNIGGDPIIA DLAKMPHLLV AGTTGSGKSV
AINTMVLSLL YKLSPKECQF IMIDPKMLEL SVYEGIPHLL TPVVTEPKKA VAALKWVVKE
MENRYRSMSI LGVRNIQGFN KAIEESISKG QRLEKQIQTG FDQETGKPTF ETIEMPAEPL
PYIVVIVDEM ADLMLVAGKD IEGYIQRLAQ MARAAGIHII MATQRPSVDV ITGVIKANFP
TRISFQVTSK IDSRTILGEQ GAEQLLGMGD MLYMMGGGKI ERVHGPFVGD KEVEMVVDYL
KSQGSPKYKI EITLDEDEEG DSIINMAGGD TDDLYSQAVA IVLRDRRPTT SYLQRCLKVG
YNKAASLIEK MEKEGILSPP NHTGKREILV ND
//
