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Database: UniProt
Entry: Q2N780_ERYLH
LinkDB: Q2N780_ERYLH
Original site: Q2N780_ERYLH 
ID   Q2N780_ERYLH            Unreviewed;       763 AA.
AC   Q2N780;
DT   07-FEB-2006, integrated into UniProtKB/TrEMBL.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   OrderedLocusNames=ELI_11845 {ECO:0000313|EMBL:ABC64461.1};
OS   Erythrobacter litoralis (strain HTCC2594).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=314225 {ECO:0000313|EMBL:ABC64461.1, ECO:0000313|Proteomes:UP000008808};
RN   [1] {ECO:0000313|Proteomes:UP000008808}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2594 {ECO:0000313|Proteomes:UP000008808};
RX   PubMed=19168610; DOI=10.1128/JB.00026-09;
RA   Oh H.M., Giovannoni S.J., Ferriera S., Johnson J., Cho J.C.;
RT   "Complete genome sequence of Erythrobacter litoralis HTCC2594.";
RL   J. Bacteriol. 191:2419-2420(2009).
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; CP000157; ABC64461.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2N780; -.
DR   STRING; 314225.ELI_11845; -.
DR   KEGG; eli:ELI_11845; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_7_5; -.
DR   Proteomes; UP000008808; 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}; Reference proteome {ECO:0000313|Proteomes:UP000008808};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        98..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        123..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          397..616
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          210..251
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         414..421
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   763 AA;  82926 MW;  B9F5B4D211993DC5 CRC64;
     MRRAAQMGGA VVLFGAMVFL GLALFSYTQT DPSPSTAAAS HDVANYMGAS GAFVAERVLF
     LFGLTGILLL PMLYIFARKL WRDVEEEDVD TETRWWRPIL MLLLAMALLS TVLSLTFDGP
     GGALPASMGG ITGLLGAGAI EAIATRFGEG LSGWIILALA LLALGGGTAL VTRVFAIDWR
     ALLTLPAFLR HVPFMPAIAL PKPRLALNRD TDAAPKPRPA AKEAVVEQPA ERRAPKIVDP
     SAPPKQATAA KAKQRDMFAN YELPSLDLLT DPGPDTAPKL DKMALERNAR LLETVLDDFN
     VKGEITAVRT GPVVTMYELE PAPGIKASRV IGLAEDIARN MSAISARVSP IPGKTVMGIE
     LPNQDRQMVN FKELASCAAF ADGKGALPMI LGKDIAGEPI VADLAAMPHL LVAGTTGSGK
     SVGLNAILLS LLYRFTPDEC RLILIDPKVL ELKTYDDIPH LLSPVVTEPH KSVRALKWAV
     EEMERRYRMM SSVNSRNISG FNEKVRTAAA KGKPLGRRVQ TGFDPETGEE IFEEEQLDYE
     PLPQIVLIVD ELADLMVTVG KEIEVLIQRL SQKSRAAGIH LIMATQRPSV DVITGVIKAN
     LPTRISFKVT SRIDSRTIFG EQGSEQLLGK GDMLYKPNTG AMIRVHGPFV SDEEVERVAD
     HWRAQGSPAY VDAVTEEPED GGGLTFEDDL TASDSPEERK YLQACQIVIE NQKASGSWLQ
     RQMGVGYNTA AKWIERMESE GLVGPANHVG RREIYRDRDG NVL
//
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