ID A0A367AQB9_9ACTN Unreviewed; 831 AA.
AC A0A367AQB9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:RBY90937.1};
GN ORFNames=DQ241_04400 {ECO:0000313|EMBL:RBY90937.1};
OS Blastococcus sp. TF02A-30.
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=2250580 {ECO:0000313|EMBL:RBY90937.1, ECO:0000313|Proteomes:UP000253175};
RN [1] {ECO:0000313|EMBL:RBY90937.1, ECO:0000313|Proteomes:UP000253175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF02A-30 {ECO:0000313|EMBL:RBY90937.1,
RC ECO:0000313|Proteomes:UP000253175};
RA Ennis N., Dharumadurai D., Sevigny J., Morris K., Simpson S., Thomas W.K.,
RA Tisa L.S.;
RT "Genome Sequence of Blastococcus sp. TF02-30.";
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 -!- 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}.
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:RBY90937.1}.
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DR EMBL; QOHJ01000002; RBY90937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A367AQB9; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000253175; 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, ECO:0000313|EMBL:RBY90937.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000253175};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 89..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 122..143
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..174
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 477..677
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 494..501
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 831 AA; 88967 MW; B3F7E7B7C9855088 CRC64;
MPARTTPTRK PPAKSRSGST AASKKRPAAK RAPNRRPPAR KKQDSGFSLW RAASGTWGLL
ARGAGGLARS VARPEEAEPL APEHRRDGVG LAVLGLAIVL GAAAWSNGIG PVGEALTDGV
RWIVGSLVMV LPVVFFFAAL RLLRRGPRPE ARGRLAIGWL CMVAAVLGIA HVVGTPADPE
AGVPGSGGLV GWAVGTPLVA GMSSAVAVVL LGLAAFFGLL VITATPVHQI PERLRELGDR
VLGRADDYED DDAYDDFDYE EEEPAPKSRR RKNSLSEDLL TTGPIDHAAY EAAPEATLVT
EPEHTQLHAP TRPPVVDRTS PPEDLPPITE PEQLSIQPVE GDYVLPALSM LRPGDPPRAR
SKANDVAIEA ISGVLEQFNI DAAVTGFTRG PTVTRYEVEL GQGVKVEKIT QLTKNMAYAV
ANDNIRILAP IPGKSAVGIE VPNTDREKVS LGDVLRSGAA KQDPHPMLVG LGKDIEGGFV
CANLAKMPHL LVAGATGAGK SSCVNSILTS LLLRATPDQL RMILVDPKMV ELTPYDGIPH
LITPIITDPK KAATALAWLV EEMEQRYQDM KSTGVRHIDD FNRKVEKGEI TAPPGSERVY
RPYPYILAIV DELADLMMVA PRDVEEHIVR ITQKARAAGI HLILATQRPS VDVVTGLIKA
NVPSRLAFST SSLTDSRVIL DQPGAEKLIG MGDALFMPIG AGKPMRVQGA FVTDAEIEAV
VEFTKRQAEP EYREEVFTAG AAGEKKEIDE DIGGDLDLLL QAVELIVTSQ FGSTSMLQRK
LRVGFAKAGR LMDLMESRGI VGPSEGSKAR DVLIKPDELE SVLFTLRGGE A
//
