ID A0A1X4NBD7_9PROT Unreviewed; 822 AA.
AC A0A1X4NBD7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=THS27_08835 {ECO:0000313|EMBL:OSQ43913.1};
OS Thalassospira sp. MCCC 1A01428.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Thalassospiraceae; Thalassospira.
OX NCBI_TaxID=1470575 {ECO:0000313|EMBL:OSQ43913.1, ECO:0000313|Proteomes:UP000193740};
RN [1] {ECO:0000313|EMBL:OSQ43913.1, ECO:0000313|Proteomes:UP000193740}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A01428 {ECO:0000313|EMBL:OSQ43913.1,
RC ECO:0000313|Proteomes:UP000193740};
RA Lai Q., Shao Z.;
RT "The draft genome sequence of Thalassospira sp. MCCC 1A01428.";
RL Submitted (MAR-2014) 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:OSQ43913.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; JFJZ01000008; OSQ43913.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X4NBD7; -.
DR STRING; 1470575.THS27_08835; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000193740; 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: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, ECO:0000313|EMBL:OSQ43913.1};
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 30..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 79..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..667
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 228..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 465..472
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 822 AA; 88352 MW; D7D0B292F5065A1E CRC64;
MSSQTNLLER GTAFLPSALV SFLKRGGIQL CGLALTAAGI ALFIMLIGFH PGDPSFNHAS
DHAYIYNPLG IFGAYFADMM LRTLGLGAAL LTALIVGWGL RLIAMRPFSW MWLRFLVLPL
ALLLMATAAS AVPRGMTWPL TVGYGGFAGD LLLGRLGMLL TLAGIPAGPV IIGLFSMVVG
MGLTLFCMAY QLSEWRAVGH VLSRIGGTVI YGVGRAIPGN SADEVAEIAP GERKGDRNAR
PRQEPSMERS EKRVAAAVER NTLSASDDAD DYDDIDNEPP VHIVAPPAAK VQPSTKASAQ
RQSSFDLGAG EYSFPPLGLL HEPSEEDYAQ IDQGALAQNA RLLETVLQDF GVKGEIVQVR
PGPVVTLYEL EPAAGVKSSR VIGLADDIAR SMSAIAARVA VVPGRNVIGI ELPNSTRETV
HLHEILASND FEKNTGKLNL SLGKDIGGSP VIADLSKMPH LLIAGTTGSG KSVGVNAMIL
SLLYKHTPEE CRFIMIDPKM LELSIYDGIP HLLTPVVTDP HKAVVSLKWA VREMEDRYRA
MSQVGVRNIA GYNKRIKEAA AKGEELTRRV QTGFDPETGK PIFEDQQLPM EALPFIVVIV
DEMADLMLVA GKDVEASIQR LAQMARAAGI HLIMATQRPS VDVITGTIKA NFPTRISYSV
TSKIDSRTIL GEMGAEQLLG QGDMLFMGQG GRLQRVHGPF VSDEEVESIV KHLRDQGDPS
YLDEVTEEPE EDPVAAYMAG GGNAGSGGGN SADDDLYNQA VGIVLREKKA STSFVQRKLS
IGYNRAARII EQMEENGLVS AANHVGKREV LIGNMDGTPF ED
//
