ID A0A0M8YD91_9ACTN Unreviewed; 828 AA.
AC A0A0M8YD91;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KOX24139.1};
GN ORFNames=ADL05_00695 {ECO:0000313|EMBL:KOX24139.1};
OS Nocardiopsis sp. NRRL B-16309.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX24139.1, ECO:0000313|Proteomes:UP000037694};
RN [1] {ECO:0000313|Proteomes:UP000037694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-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:KOX24139.1}.
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DR EMBL; LGEC01000002; KOX24139.1; -; Genomic_DNA.
DR RefSeq; WP_053614850.1; NZ_LGEC01000002.1.
DR AlphaFoldDB; A0A0M8YD91; -.
DR STRING; 1519494.ADL05_00695; -.
DR PATRIC; fig|1519494.3.peg.153; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000037694; 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:KOX24139.1};
KW Cell division {ECO:0000313|EMBL:KOX24139.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000037694};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 31..54
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..93
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 99..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 144..165
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 197..219
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..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..283
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..319
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 828 AA; 87759 MW; 0D947ECB51F1B092 CRC64;
MPARASSGGS GRKKPASRKP AAGRRMPDGP IAFAVTMFGQ FLLVLWKLVA HTVGGAARAV
GRSARDLDPD LRRDGAGLVL LAAGILVAGA VWWQSEGPLL AYTRLAVAGT FGTFSPILPL
LFLPVAVKLM RTPATGREGD TGRLFIGFSS IMLGLLGLIH IGHGIPQPSE GMAALRESGG
LIGFVASGPL SAVITPWLTG LLLVLVLLFG ILVVTATPIR RIPERLQTLF GALLERDTGP
DAGIGILGAD AEKRKKPAKP RRKAPRSAEE SVAGDHERPY DSPVLPGEPE PVAPALTDEE
EAAAAPAGRR GKGRAKTKDP APDPTPAPGA TEQLSIPSRV VEGDYELPVA SMLKPGSAAK
PRTKANDEMV AALSGVLTQF KLDADVTGFT RGPTVTRYEI ELGPAVKVEK VTALAKNISL
AVKSADVRIL SPIPGKSAIG VEIPNTDKDI VSLGDVLRSP AATSDDHPML VGLGKDVEGS
NVVANLAKMP HVLVAGATGA GKSTCINGLI TSLMMRSTPD EVRMILVDPK RVELTMYEGI
PHLITPIITS PKKAAEALQW VVGEMDRRYD DLAASGYRHV DDFNAAVRKG ELTAPPGSER
VYEPYPYLLV IVDELADLMM VAPRDVEDAV VRITQLARAA GIHLVLATQR PSVDVVTGLI
KANVPSRLAF ATSSLSDSRV ILDQPGAEKL VGKGDALFLP MGAGKPIRLQ NAWVSEKEIR
AIVDHCKKQS EPSYREDVAV PETKKKEIDE DIGDDLDLLL QAVELVVTTQ FGSTSMLQRK
LRVGFAKAGR LMDLMESRDV VGPSEGSKAR DVLVTPDELP GVLADIRG
//
