ID A0A370BEL8_9ACTN Unreviewed; 954 AA.
AC A0A370BEL8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:RDG38263.1};
GN ORFNames=DVH02_10220 {ECO:0000313|EMBL:RDG38263.1};
OS Streptomyces corynorhini.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2282652 {ECO:0000313|EMBL:RDG38263.1, ECO:0000313|Proteomes:UP000253741};
RN [1] {ECO:0000313|EMBL:RDG38263.1, ECO:0000313|Proteomes:UP000253741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AC230 {ECO:0000313|EMBL:RDG38263.1,
RC ECO:0000313|Proteomes:UP000253741};
RA Dunlap C.;
RT "Streptomyces species from bats.";
RL Submitted (JUL-2018) 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:RDG38263.1}.
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DR EMBL; QQNA01000064; RDG38263.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370BEL8; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000253741; 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:UP000253741};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 110..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..166
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 178..200
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 231..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 596..801
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 39..53
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 618..625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 954 AA; 101014 MW; 2AFAF30CDE74BAB3 CRC64;
MASRTSGNGS QGTAGTAKPR AGRTSGAAKA APAKKTAAKK TAPAKKAPAK KTAAKKTAAK
PAPRPAPSPT GGVYRVVRAV WLGAAHGVGA MFRGIGRGAK GLDPAHRKDG VALLLLGIAL
VIAAGTWSNL HGPVGDLVEM LITGAFGRLD LLVPILLGVV AVRLILYPEK PDANGRIVIG
LSALIIGVLG LVHIACGAPG RGEGTAAMQD AGGLIGWAAS MPLIFTTGEV LAVPLLLLVT
VFGLLVVTAT PVNAIPRRLR QLGVRLGIVE PTHERDRFDD GYDERYDDGP FDDDERYDEQ
WRQALPSAGA RRSPGRRGGP PREYDADQAE SEALAKRRRP RRPSVQPSME RSMDPVDVAA
AAAAALDGAV LNGMPPSPIV ADLTQGVSVE RTRSPGQRPG ERADRPAPAD DAQSSAPVPA
AREERSRPAG ARPGAAPVAD LTKPAPALDK PLPARAEQLQ LRGDITYSLP SLDLLERGGP
GKTRSAANDT VVASLTNVFQ EFKVDAAVTG FTRGPTVTRY EVELGPAVKV ERITALTKNI
AYAVASPDVR IISPIPGKSA VGIEIPNTDR EMVNLGDVLR LADAAEDDHP MLVALGKDVE
GGYEMANLAK MPHLLVAGAT GSGKSSCINC LITSVMVRAT PEDVRMVLVD PKRVELTAYE
GIPHLITPII TNPKRAAEAL QWVVREMDLR YDDLAAYGYR HIDDFNKAVR DGKVKVPEGS
ERELSPYPYL LVIVDELADL MMVAPRDVED AIVRITQLAR AAGIHLVLAT QRPSVDVVTG
LIKANVPSRL AFATSSLADS RVILDQPGAE KLIGKGDGLF LPMGANKPTR MQGAFVTEDE
IQAVVQHCKD QMAPVFRDDV VVGTAKKKEI DEDIGDDLDL LCQAVELVVS TQFGSTSMLQ
RKLRVGFAKA GRLMDLMESR NIVGPSEGSK ARDVLVKADE LDGVLGVIRG ENPA
//
