ID B5JY79_9GAMM Unreviewed; 791 AA.
AC B5JY79;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=GP5015_1357 {ECO:0000313|EMBL:EDY85423.1};
OS gamma proteobacterium HTCC5015.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY85423.1, ECO:0000313|Proteomes:UP000004692};
RN [1] {ECO:0000313|Proteomes:UP000004692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX PubMed=20472792; DOI=10.1128/JB.00510-10;
RA Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequence of the novel marine member of the Gammaproteobacteria
RT strain HTCC5015.";
RL J. Bacteriol. 192:3838-3839(2010).
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; DS990618; EDY85423.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JY79; -.
DR STRING; 391615.GP5015_1357; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_6; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000004692; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; 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:EDY85423.1};
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:UP000004692};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 426..641
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 252..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 706..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 443..450
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 791 AA; 86800 MW; D7288E09454BEC87 CRC64;
MSSAKKSAAT RGAARKVKAK RTLSPWVKRR LLESALCLLV ALAVYVLLVL WSYDPSDSGF
SHTGPRDRAA NLGGIIGAHI SDLLLWVFGY LAYLVPIMGG YSAWLMVRTR SAERSFDGHL
LAVRWVGFVM MVVSGCGLAG IHFSVNEGAL PAQLAGGLLG QQVGFGLVDS LNIVGTTVLL
LALFLASIPM FTGISWLKVI DYTGRYALLA GHYALQVSSS VMDRWRDRRQ YSKARQERKE
LFEEAQKEVK ERKAKAPKRK IEPKMAPEKR VSEREFKEQQ IPLFEAPPNT ELPPISLLDD
PKEQTFGYSA EALEAMSDLL EHKLNDFNVT AEVVNVLPGP VITRFEIQPA PGTKASKITG
LSKDLARSMS VVSVRVVEVI PGKSVVGIEI PNETREIISF QEIMRSKSYE KLKSPLAIGL
GKDISGVPVS ADLGKMPHLL VAGTTGSGKS VAINAMLLSL LYKATAEEVR LILIDPKMLE
LNVYEGIPHL LCPVVTDMKD ATNALRWSVG EMERRYKLMS QLGVRNLAGY NRKVREAINK
GEPISDPMYK REEAFDPDAP PPTLEPMSHI VIIIDEFADM MMVVGKKAEE LIARLAQKAR
AAGIHMILAT QRPSVDVITG LIKANVPTRI AFQVSSRVDS RTILDQMGAE QLLGHGDMLY
YQPGVTNTPE RVHGAFVDDH EVHEVVEHLK RTSGEPEYID SILEESSEPL PGMSPEAAGG
GGEELDPLYD QAVRVVTESR KASISYVQRR LKVGYNRAAS MLEVMEEQGV VTKAEGNGSR
EVLAPPPPPA D
//
