ID A0A1M6E7E5_9ACTN Unreviewed; 829 AA.
AC A0A1M6E7E5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SHI81416.1};
GN ORFNames=SAMN05421803_102184 {ECO:0000313|EMBL:SHI81416.1};
OS Nocardiopsis flavescens.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=758803 {ECO:0000313|EMBL:SHI81416.1, ECO:0000313|Proteomes:UP000184452};
RN [1] {ECO:0000313|EMBL:SHI81416.1, ECO:0000313|Proteomes:UP000184452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.5723 {ECO:0000313|EMBL:SHI81416.1,
RC ECO:0000313|Proteomes:UP000184452};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; FQZK01000002; SHI81416.1; -; Genomic_DNA.
DR RefSeq; WP_073375862.1; NZ_FQZK01000002.1.
DR AlphaFoldDB; A0A1M6E7E5; -.
DR STRING; 758803.SAMN05421803_102184; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000184452; 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:UP000184452};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 30..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..128
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 140..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 193..214
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 479..679
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 240..332
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 250..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 496..503
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 829 AA; 88078 MW; 90E652DADC4BE53D CRC64;
MSPRASSGGS ARKKPAARRP AAKRMPDGPI AFAVTMFGQF LLVLWKLVAH TVGGAARAVG
RSARDLDPDL RRDGAGLLLL ATGVLVAAAV WWESDGPLPE YTRLVVVGGF GTFSPILPLL
FLPLAIRLMR TPGASREGDA GRLFIGTSAI LLGLLGLIHI ANGIPQPSEG LEALQRAGGL
IGFVASGPLS AVITPWLTGV LLALVLVFGI LVVTSTPIRR IPERLHTLFG ALMERDAGPD
SGIGILGAEP EKKPARRRRA PKKAAAEAAS AETVAGDRER PYDSPVLPEE SLVPALTDEE
EAQARAGAAE DGKKGRKKLT VPDPTPPPAV AEQLSIPSRV VEGDYELPVP ALLKPGSPVK
PRTKANDDVV EALTGVLTQF GIDAEVTGFT RGPTVTRYEI ELGPAVKVEK VTALTKNISL
AVKSADVRIQ SPIPGKSAIG VEIPNTDKDI VSLGDVLGST VATSDDHPML VGLGKDVEGT
NVVANLAKMP HILVAGATGA GKSTCINGLI TSLMMRAAPD EVRMILVDPK RVELTMYEGI
PHLITPIITN PKRAAEALQW VVGEMDRRYD DLAASGYRHI DDFNAAVRTG ELTTPPGSER
VYEPYPYLLV IVDELADLMM VAPRDVEDSV VRITQLARAA GIHLVLATQR PSVDVVTGLI
KANVPSRLAF ATSSLADSRV ILDQPGAEKL VGKGDALFLP MGAGKPIRLQ NAWVSEKEIR
AIVDHCKKQA EPSYREDVAV ADTRKKEIDE EIGDDLDLLL QAVELVVTTQ FGSTSMLQRK
LRVGFAKAGR LMDLMESRDV VGPSEGSKAR DVLVTPEDLP AVLTDIRGG
//
