ID A0A1H0GHK6_9PSEU Unreviewed; 757 AA.
AC A0A1H0GHK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SDO06380.1};
GN ORFNames=SAMN05421507_1011212 {ECO:0000313|EMBL:SDO06380.1};
OS Lentzea jiangxiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=641025 {ECO:0000313|EMBL:SDO06380.1, ECO:0000313|Proteomes:UP000199691};
RN [1] {ECO:0000313|EMBL:SDO06380.1, ECO:0000313|Proteomes:UP000199691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6609 {ECO:0000313|EMBL:SDO06380.1,
RC ECO:0000313|Proteomes:UP000199691};
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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination.
CC {ECO:0000256|ARBA:ARBA00024986}.
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; FNIX01000001; SDO06380.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0GHK6; -.
DR STRING; 641025.SAMN05421507_1011212; -.
DR Proteomes; UP000199691; 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};
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 30..48
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 400..600
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 189..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 417..424
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 757 AA; 81361 MW; AD53951780E4ABCB CRC64;
MWGALGRGVG TVVRGITGTK GLEPEHRRDG LGLFLIALAF ITGTGVWWQA GGPVGRWVDV
AVRSSVGFPA VFVPVVLLGI GVVLMSTDAK PEERFRLVVG GTLISIGVLG MFHLIGGLPM
DPLARRDAGG ALGYLAGGFL AQGLTPWVAG PLLVMIFVFG LLCVLHWPVR EVPQRLRALV
HRERTAEPFD FEDEPEEEPK PVRLRRPSRR RQAAETPVEE PQAELPLDEP AEPAPKPAPK
PAPAAKKAAA AAPAPAMAVR AVEGDYQLPP PTILKDGDAP KARSKANDQM IDAITGVLDQ
FSIDAQVTGF TRGPTVTRYE VELGPGVKVE KITALTKNIA YAVATDNVRL LAPIPGKSAV
GIEVPNSDRE MVRLGDVLRA PSTLQDTHPM VIGLGKDIEG HMVTANLTKM PHLLVAGSTG
SGKSSFVNSM LVSLLARATP DEVRMILIDP KMVELTPYEG IPHLITPIIT QPKKAAAALA
WLVEEMEQRY QDMQVNRVRH IDDFNRKVKS GEIAAPPGSE RVYRPYPYIM AIVDELADLM
MTAPRDVEDA IVRITQKARA AGIHLVLATQ RPSVDVVTGL IKTNVPSRLA FATSSLTDSR
VILDQPGAEK LIGMGDGLYL PMGAGKPVRI QGAFVGDEEI SQIVDFTKNQ AQPEYTDGVT
AAKAGEKKEI DADIGDDLEL LVQATELIVT SQFGSTSMLQ RKLRVGFAKA GRLMDLLETR
GVVGPSEGSK AREVLIKPDE LENVIYLMRG GGPADGE
//
