ID A0A1U7MU37_9MICO Unreviewed; 901 AA.
AC A0A1U7MU37;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:OLT23319.1};
GN ORFNames=BJF81_11355 {ECO:0000313|EMBL:OLT23319.1};
OS Ornithinimicrobium sp. CNJ-824.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Ornithinimicrobiaceae; Ornithinimicrobium.
OX NCBI_TaxID=1904966 {ECO:0000313|EMBL:OLT23319.1, ECO:0000313|Proteomes:UP000185694};
RN [1] {ECO:0000313|EMBL:OLT23319.1, ECO:0000313|Proteomes:UP000185694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNJ-824 {ECO:0000313|EMBL:OLT23319.1,
RC ECO:0000313|Proteomes:UP000185694};
RX PubMed=27902408; DOI=10.1099/mic.0.000386;
RA Schorn M.A., Alanjary M.M., Aguinaldo K., Korobeynikov A., Podell S.,
RA Patin N., Lincecum T., Jensen P.R., Ziemert N., Moore B.S.;
RT "Sequencing rare marine actinomycete genomes reveals high density of unique
RT natural product biosynthetic gene clusters.";
RL Microbiology 162:2075-2086(2016).
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 -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC {ECO:0000256|ARBA:ARBA00025923}.
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:OLT23319.1}.
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DR EMBL; MKKA01000006; OLT23319.1; -; Genomic_DNA.
DR RefSeq; WP_075957078.1; NZ_MKKA01000006.1.
DR AlphaFoldDB; A0A1U7MU37; -.
DR STRING; 1904966.BJF81_11355; -.
DR Proteomes; UP000185694; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; 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:0000256|ARBA:ARBA00023306};
KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000313|EMBL:OLT23319.1};
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:UP000185694};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..154
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 467..667
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 208..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 812..901
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..306
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 484..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 901 AA; 96162 MW; 5680641F6A041BC5 CRC64;
MTDTARDLEP EHRRDGAGFL LLALALVVAL REWWGLDGMF GDAVHAVAAG TFGRVALVLP
VVLLFFAVRL FRRPGEQQAT NRMSIGTVAL LLAGSGLTHL ATGAPDYAEG PAVMQASGGI
LGFIASSMLS AAITATGAAV VLGLLAVFGF LVLTRTPVHR IPDRLRELEQ QLFDSARFDR
VDPVTGEVLP RRRRSRAHLD ERDGDVAFEQ AAQVDGTAKG RSLRAGARAD AAQAGADAPA
GAGSRDGSPA RGRRAGAPAE AGATAARTAQ GSAPGRAGNR GRAEGDRTEE IPAVRPGQKR
PDKVPSKPQL EAPPTNPLPQ RVEQLQLAGD VTYTLPDPSV LKPGAPHKER SEANDRVVDA
LTGVLDDFNI DAQVTGFMRG PTVTRYEVEL GPGVKVERIT ALSKNIAYAV ASADVRILSP
IPGRSAVGVE IPNTDRENVN LGDVLRSQAA RNNTHPMVMG VGKDVEGGYV IANLAKMPHL
LVAGATGSGK SSFVNSMITS ILMRSTPDEV RMILVDPKRV ELTAYEGIPH LITPIITNPK
KAAEALAWVV KEMDHRYDDL SAFGYKHVDD FNKAVRAGKI TPPPGSEREL HPYPYLLVVV
DELADLMMVA PRDVEESVVR ITQLARAAGI HLVLATQRPS VDVVTGLIKA NVPSRMAFAT
SSLADSRVVL DQPGAEKLIG QGDALFLPMG ASKPMRIQGA WVAESEVHDV VVHVTGQLQP
RYVEEVVAAP AKKQVDEDIG DDLELLLQAA EQVITTQFGS TSMLQRKLRV GFAKAGRLMD
LMESRGIVGP SEGSKARDVL VKPDDMEETL ALLRGDDPPP RPELETDSAP FDALAAEVVD
EGGPVDEAWD EETGAEPTPP VIGRNPAYDG DPVSGSRVEE AEDEESEDAW GLTDRGGRER
Y
//
