ID A0A1I5KKL5_9SPHN Unreviewed; 779 AA.
AC A0A1I5KKL5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=SAMN04488060_0292 {ECO:0000313|EMBL:SFO85196.1};
OS Qipengyuania nanhaisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Qipengyuania.
OX NCBI_TaxID=604088 {ECO:0000313|EMBL:SFO85196.1, ECO:0000313|Proteomes:UP000199331};
RN [1] {ECO:0000313|Proteomes:UP000199331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.7715 {ECO:0000313|Proteomes:UP000199331};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; FOWZ01000001; SFO85196.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5KKL5; -.
DR STRING; 604088.SAMN04488060_0292; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000199331; 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; IPR036259; MFS_trans_sf.
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; SSF103473; MFS general substrate transporter; 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 76..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 114..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 414..633
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 228..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 431..438
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 779 AA; 84898 MW; B2B8F7F1A80709DE CRC64;
MATRAGAKPD WRAAFRRSLR RATHMAGAGL LLVLLVFLTL ALASYTQTDP SASTAASGTT
ISNWMGASGA WAAERAYFFF GLPALLLLPL IWISARRLWT GVEDADEEET PGRWWGPFGL
LLVAMLLLGT VVSLLFESSP GPFPAGGGGL AGLLGAGGID AVATRFGGGF SGWITGALGL
VALAGGLALV TKVFALDWAQ FFTLPKLFER KEVETDIDLP LAPKKTKRAR RKAEDIDDEE
DEEARRAPRR SPEIADPKPA PVRSQPAKAK QRDMFANYQL PSHDLLDDPP VHAAQKLDKI
ALERNARLLE NVLDDFNVKG EITAVRAGPV VTMYELEPAP GIKASRVVGL AEDIARNMSA
ISARVSPIPG KTVIGIELPN ADRQMVSYKE LSTSAAFVDS RGSLPMILGK DIGGEPIIAD
LAAMPHLLVA GTTGSGKSVG LNAILLSLLY RFTPDECRLI LIDPKVLELK TYDDIPHLLS
PVVTEPAKSV RALKWAVEEM EKRYRMMSSV NSRNIAGFNE KVKAAAAKGK PLGRRVQTGF
DPETGEELYE EEQLDYEPLP LIVLIVDELA DLMVTVGKEI EVLIQRLSQK SRAAGIHLIM
ATQRPSVDVI TGVIKANLPT RISFKVTSRI DSRTILGEQG AEQLLGKGDM LYKPNTGAMI
RVHGPFVSDE EVEKVADHWR AQGKPDYVDA VTEEPEDGGF NFEDEFTASD NPDERKYRQA
CQIVIENQKA SGSWLQRQMG VGYNTAAKWI ERMESEGLVG PANHVGRREI YRDQDGNPI
//
