ID A0A101SKQ4_9ACTN Unreviewed; 904 AA.
AC A0A101SKQ4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KUN75518.1};
GN ORFNames=AQJ64_42310 {ECO:0000313|EMBL:KUN75518.1};
OS Streptomyces griseoruber.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN75518.1, ECO:0000313|Proteomes:UP000052982};
RN [1] {ECO:0000313|EMBL:KUN75518.1, ECO:0000313|Proteomes:UP000052982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN75518.1,
RC ECO:0000313|Proteomes:UP000052982};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT for the species Streptomyces griseoruber.";
RL Submitted (OCT-2015) 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:KUN75518.1}.
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DR EMBL; LMWW01000078; KUN75518.1; -; Genomic_DNA.
DR RefSeq; WP_055634165.1; NZ_LIQS01000177.1.
DR AlphaFoldDB; A0A101SKQ4; -.
DR STRING; 1943.AQJ64_42310; -.
DR Proteomes; UP000052982; 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 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; 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}; Cell cycle {ECO:0000313|EMBL:KUN75518.1};
KW Cell division {ECO:0000313|EMBL:KUN75518.1};
KW 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 165..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 551..751
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 28..42
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 568..575
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 904 AA; 95669 MW; 6E59E2C21151444D CRC64;
MASRPSAAKK QPAKKAAAPA KAPAKKAAAK KAPARKAPAK KAAAKKAAPA PKPAPSPTGG
IYRLVRALWL GLAHAVGAVF RGIGNGAKNL DPAHRKDGVA LLLLGMALIV AAGTWADLKG
PVGDLVEILV TGSFGRLDLL VPILLAVIAV RFIRHPEQPD ANGRIVIGLS ALVIGVLGQV
HIACGAPARS AGMQAIRDAG GLIGWGAATP LTYTMGEVLA VPLLVLLTVF GLLVVTATPV
NAIPQRLRQL GVRLGVLDDP EADDELSDDD ARYDEQWREG LPGRPRRRSG GPRAYDPDGA
EREALSERRG RPRRSAVPQP AQDRELDAVD IAAAAAADLD GVVMHGLPPS PIVADLTQGV
RGGDREATAP TPVPAARPKQ EMLTGGAVPD LTKAPPEEIR DLPPRAEQLQ LSGDITYSLP
SLDLLERGGP GKARSAANDA VVASLTNVFT EFKVDAAVTG FTRGPTVTRY EVELGPAVKV
ERITALTKNI AYAVASPDVR IISPIPGKSA VGIEIPNTDR EMVNLGDVLR LADAAEDDHP
MLVALGKDVE GGYVMANLAK MPHILVAGAT GSGKSSCINC LITSVMVRAT PEDVRMVLVD
PKRVELTAYE GIPHLITPII TNPKRAAEAL QWVVREMDLR YDDLAAYGFR HIDDFNEAIR
NGKVKPPEGS ERELQPYPYL LVIVDELADL MMVAPRDVED AIVRITQLAR AAGIHLVLAT
QRPSVDVVTG LIKANVPSRL AFATSSLADS RVILDQPGAE KLIGKGDGLF LPMGANKPTR
MQGAFVTEAE VAAVVQHCKD QMAPVFRDDV TVGSKQKKEI DEDIGDDLDL LCQAAELVVS
TQFGSTSMLQ RKLRVGFAKA GRLMDLMESR NIVGPSEGSK ARDVLVKPDE LDGVLAVIRG
ESAG
//
