ID A0A1H2YL12_9RHOB Unreviewed; 940 AA.
AC A0A1H2YL12;
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=SAMN05444336_103170 {ECO:0000313|EMBL:SDX05932.1};
OS Albimonas donghaensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Albimonas.
OX NCBI_TaxID=356660 {ECO:0000313|EMBL:SDX05932.1, ECO:0000313|Proteomes:UP000199118};
RN [1] {ECO:0000313|EMBL:SDX05932.1, ECO:0000313|Proteomes:UP000199118}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17890 {ECO:0000313|EMBL:SDX05932.1,
RC ECO:0000313|Proteomes:UP000199118};
RA de Groot N.N.;
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; FNMZ01000003; SDX05932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2YL12; -.
DR STRING; 356660.SAMN05444336_103170; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000199118; 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: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; 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};
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:UP000199118};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 91..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..138
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 171..193
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 577..796
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 233..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 369..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..315
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 594..601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 940 AA; 101864 MW; 2EF8E0800A700C09 CRC64;
MALFSRSDLD DYEREPRDSF LPESWSEALR RRAAELAGLA LAGLAVAAAL MLASYSSEDP
SFFNMSGGDA SNWLGMAGAY AADPLMRTLG LASWMLPLLI GVWGWRLVTH EGEHRAWSRL
LLSPLAVLAV AAALSTHIPP AAWPHPYGLG GLIGDGAGRT LAQQAPWPLE LTLLALSLSL
GFCAVALSLL SLGVDWEELA ALRRWMADGL IWALGLVFAL VAFIASRRRK PAEPRSSRLG
APRPIGAAAR HEPAMEEDED PLYDDEEMDE PQLSTRRAAR AEPRAEPRAE PRAEPRAEPR
VRAEPEADAP LRAEPSVVDR IRSVARRIEP APAPLHDHDP DFGGYDDDAD YAAPVAARPE
PVARVAVPAP APAPVSAGPR EPSVSSRALG DDYDDADPAP IPDPVPRAQV APPVRAPAQS
RRAAAEAQPM LAFDDQADDA WSAPPLSLLQ NPARIERPHH STEALEENAR MLEAVLDDYG
IRGEIVKVSP GPVVTMYELE PAPGLKASRV IGLADDIARS MSALAARVST VPGRSIIGIE
LPNEIREKVL LRELFAARAF GDAKERLLIA LGKDIAGAPI VANLARMPHL LIAGTTGSGK
SVAINVMILS LLYRLSPKEC RMIMIDPKML ELSVYDGIPH LLSPVVTDPK KAVVALKWTV
AEMEDRYRKM SRMGVRNIEG YNQRVRDAVA KGEAFTRTVQ TGFDDDTGEP VYETQEFEPE
ELPFIVVVVD EMADLMMVAG KEIEACIQRL AQMARASGIH IIMATQRPSV DVITGTIKAN
FPTRISFQVT SKIDSRTILG EMGAEQLLGM GDMLYMAGGG RVTRVHGPFV SDEEVEEVVM
HLKAQGEPSY IGGVTDGPDE EQASEIDAVL GLSGDETESE LYDRAVAIVA RDRKCSTSYI
QRKLAIGYQR AARLVEQMEE QGVVSPANKV GKREIMVGEV
//
