ID A0A1G7ZN91_9ACTN Unreviewed; 854 AA.
AC A0A1G7ZN91;
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:SDH10037.1};
GN ORFNames=SAMN05660324_4290 {ECO:0000313|EMBL:SDH10037.1};
OS Klenkia brasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Klenkia.
OX NCBI_TaxID=333142 {ECO:0000313|EMBL:SDH10037.1, ECO:0000313|Proteomes:UP000198863};
RN [1] {ECO:0000313|EMBL:SDH10037.1, ECO:0000313|Proteomes:UP000198863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44526 {ECO:0000313|EMBL:SDH10037.1,
RC ECO:0000313|Proteomes:UP000198863};
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; FNCF01000009; SDH10037.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7ZN91; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000198863; 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 99..118
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 166..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 212..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..700
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..58
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 255..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 854 AA; 90608 MW; 5664A1DC58092562 CRC64;
MPARSTTSTR RSASGGSSRS RPATTAAKKK APAKRAPAKR GSTTAARRPA PRRRSVGAGL
WSAASGTWSL LARGAGGLAR SVARPEEAQP LAPEHRRDGV GLAVLGLAIV LGVTAYVGDV
GPVGSAIVDA FRWAFGALTY LLPVVLLLAA LRLLRHGPRP EARGRLVIGW VCIVLPVLGI
AHLVTGSPTG DERHAGGGLV GWAVGNPVGA GVGTAVGVAL FLLVVFFGVL VVTATPVHQV
PERLRGFVDR VTGRGEDEYD EDEYEDDEFV PDLGEDADPP KPRAVRRGRA QAAMDALTSA
ADSTETGVID QGPVEGAGDA VALEPTAGTA LRRPAVVEDR TRRVEPELPP ITEPEQMVIE
PVEGDYVLPS LNSLRPGDPP KARSKSNDIA IEAITGVLEQ FNIDAAVTGF TRGPTVTRYE
VELGPAVKVE KITALTRNLA YAVANDNIRI LAPIPGKSAV GIEVPNVDRE KVSLGDVLRS
GAAKQDPHPM LVGLGKDIEG GFVCANLAKM PHLLVAGATG AGKSSCVNSL LTSLLLRATP
DQLRMILIDP KMVELTPYDG IPHLITPIIT DPKKAATALA WLVEEMEQRY QDMRATGVRH
VDDFNRKVER GEVTAPPGSE RVYRPYPYIL AIVDELADLM MVAARDVEES IVRITQKARA
AGIHLVLATQ RPSVDVVTGL IKANVPSRLA FSTSSLTDSR VILDQPGAEK LIGMGDALFL
PIGAGKPLRV QGAFVSDAEI EAVVEFTKRQ AEPDYREEVF TAAAGEQKEI DEDIGGDLEL
LVQAVELVVT SQFGSTSMLQ RKLRVGFAKA GRLMDLMESR GIVGPSEGSK ARDVLLKPDE
LEGALYLLRG GVEG
//
