ID A0A0N1L1R1_9SPHN Unreviewed; 820 AA.
AC A0A0N1L1R1;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=IP65_16980 {ECO:0000313|EMBL:KPF52257.1};
OS Novosphingobium sp. AAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF52257.1, ECO:0000313|Proteomes:UP000037880};
RN [1] {ECO:0000313|EMBL:KPF52257.1, ECO:0000313|Proteomes:UP000037880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF52257.1,
RC ECO:0000313|Proteomes:UP000037880};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF52257.1}.
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DR EMBL; LJHO01000012; KPF52257.1; -; Genomic_DNA.
DR RefSeq; WP_054132398.1; NZ_LJHO01000012.1.
DR AlphaFoldDB; A0A0N1L1R1; -.
DR STRING; 1523413.IP65_16980; -.
DR PATRIC; fig|1523413.3.peg.1020; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000037880; 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:KPF52257.1};
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:UP000037880};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 92..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 456..675
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 730..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 820 AA; 88251 MW; 6B86B229534DEC41 CRC64;
MASRALTPNR STAPGGGKLG PGRGNPNWRA VLRRSFRRSF ELIGGATLFG AMVFLALALV
SYTQTDPSGS TASGSPVDNW MGLPGAWAAE RVLVLFGLPG GLLVPLLFVF ARRLWDAAGD
LIDVDEDEEA PAPEPAWWRL SLGLSVAMML SGTALALAFT GPGGSLPAGF GGATGLLGAA
GVRALAGLVP VAQGWIILAI ALLAFGGGLF LTGRVFALDW ARLLSIPAFL RRTPREAAAD
GAPARQRRAP KAKAAAGGDA LLADDDDGAD DDAPPFDTRA PVIPADAAAP RRPTEISDPQ
RTPAPAAKAQ ARQSDLFDKF ALPAIDILEE IPASAQPKID KLALERNARL LENVLDDFNV
KGEITAVRTG PVVTMYELEP APGIKASRVI GLADDIARNM SAVSARVSAI PGRTVMGIEL
PNQIRDMVSF RELVACDKFV NAKGLLPIIL GKDIAGEPIV ADLATMPHLL VAGTTGSGKS
VGLNCILLSL LYRLTPAQCR MILVDPKVLE LKSYDDIPHL LSPVVTEPAK AVRALKWAVE
EMERRYRQMS SIGVRNLSGF NEKVRAAQAK GKPLGRRIQV GFDPETGEEL FEEQQLEYQV
LPQIVVIVDE LADLMVSVGK EIEVLIQRLS QKSRAAGIHL IMATQRPSVD VITGVIKANL
PTRISFAVTS RIDSRTILGE QGAEQLLGKG DMLYKPSTDP IKRVHGPFVS DEEVERVADH
WRGQGKPEYV DSVTEEPEEG SYGFDELDTS DNPEDRKYRQ VCQLVFESQK ASASWIQRQM
GVGYNTASKW VERMEQDGLV GPANHVGRRE IYRDKDGNPL
//
