ID A0A1R1SQV8_9ACTN Unreviewed; 956 AA.
AC A0A1R1SQV8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:OMI40700.1};
GN ORFNames=SPAR_04611 {ECO:0000313|EMBL:OMI40700.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI40700.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI40700.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI40700.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) 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 -!- 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:OMI40700.1}.
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DR EMBL; ASQP01000069; OMI40700.1; -; Genomic_DNA.
DR RefSeq; WP_065965305.1; NZ_ASQP01000069.1.
DR AlphaFoldDB; A0A1R1SQV8; -.
DR STRING; 67365.GCA_001704635_00317; -.
DR Proteomes; UP000186168; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 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; 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; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000186168};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 112..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 142..167
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..257
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 603..803
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..73
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 297..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 620..627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 956 AA; 100174 MW; 86AC2F489467402B CRC64;
MASRTSGKGS QSTAGTSKKR AGPSGGAAKK APAKKAVARK APVKKSAAPV KKAAPRKAAA
KAAPPKPAPS PTSGVLRAAR AVWMGMARGV AALFRGIGRG AKGLDPAHRK DGSALLLLAL
ALIVAVGTWS NLRGPVGDLV EVLVTGAFGR LDLIVPILLG AIAVRLILHP EKPEANGRIV
IGLSALVIGV LGQVHIACGA PGRGQGTQAI QDAGGLIGWA ASRPLIVAMG EVLAVPLLVL
LTVFGLLVVT ATPVAAIPHR LRLLGIRLGL VREHPVGYQV DDDYAAYERD DAEYAQEWRE
TPARRPRRAS LDKGGPQGAD DPERAEEEAL RKRRRPRRGQ SAQPPLDRPM DAVDVAAAAA
AALDGAVLHG VQPSPLVAGL SSGISTTDRI PGSDTGGVPG ARDAEQAGAP GAPAGKGKRP
GRPKAAEGAE GAEGERTALV PDLTRPTPEP SEPLPPRAEQ LQLSGDITYA LPSLDLLERG
GPGKTRSAAN DAVVASLSTV FSEFKVDASV TGFTRGPTVT RYEVELGPAV KVERITALTK
NIAYAVASPD VRIISPIPGK SAVGIEIPNT DREMVRLGDV LRSADAVGDD HPMIVALGKD
VEGGYVSHNL ATMPHVLVAG ATGSGKSSCI NCLITSVMVR ATPDDVRMVL VDPKRVELTA
YEGIPHLITP IITNPKRAAE ALQWVVREMD LRYDDLAAFG FRHVDDFNAA VRAGKVKQPE
GSERELKPYP YLLVIVDELA DLMMVAPRDV EDSIVRITQL ARAAGIHLVL ATQRPSVDVV
TGLIKANVPS RLAFATSSLA DSRVILDQAG AEKLIGKGDS LFLPMGASKP VRMQGAFVTE
EEVAAVVEHC KAQMAPVFRD DVTVGTAKKK EIDEDIGDDL DLLCQAAELV VSTQFGSTSM
LQRKLRVGFA KAGRLMDLME SRGVVGPSEG SKARDVLVKP EELDGVLAVI RGEAHS
//
