ID A0A0R2TXT9_9ACTN Unreviewed; 776 AA.
AC A0A0R2TXT9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KRO91975.1};
GN ORFNames=ABS08_04330 {ECO:0000313|EMBL:KRO91975.1};
OS Actinobacteria bacterium BACL4 MAG-120507-bin0.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1655610 {ECO:0000313|EMBL:KRO91975.1, ECO:0000313|Proteomes:UP000051564};
RN [1] {ECO:0000313|EMBL:KRO91975.1, ECO:0000313|Proteomes:UP000051564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BACL1 MAG-120507-bin0 {ECO:0000313|EMBL:KRO91975.1};
RA Hugerth L.W., Larsson J., Alneberg J., Lindh M.V., Legrand C., Pinhassi J.,
RA Andersson A.F.;
RT "Metagenome-Assembled Genomes uncover a global brackish microbiome.";
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 -!- 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:KRO91975.1}.
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DR EMBL; LICQ01000118; KRO91975.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2TXT9; -.
DR Proteomes; UP000051564; 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:KRO91975.1};
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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 54..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 118..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..189
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 427..627
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 444..451
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 776 AA; 84550 MW; 7075FFD808DDF346 CRC64;
MAKKKSKAKK IRIFAPIIRG LSSIWRFVSK ILGSAVRFIF RSSKELDPTH QRDGIAFFIF
ILALIFSAGI WFKLDNFLGK STYAFLFGAV GQLAYLVPLI FIYFAYRIFK SPDESGDTGR
ITIGTLLLLI SITALIHIIN GSVGTGATAI QQGGGWIGYG VSTSLIAVVT EVLAIPILLI
VLLFGLLIVT KTSLSKLFTQ IKRLFRFSGS GIGKLRQRRA QKLVAEDFEV SESPPFETPL
VKDLVQEFEP QQEEFEIELE DFDQITQPIP IIQPVKHENS RPQQLLLSSD VKYELPPLDL
LRGGPAAKGK SKANEAVVAA LKQVFEQFNV DAQVTGFMRG PTVTRYEVEL GNGVKVEAIS
ALSKNIAYAV ASGEIRILSP IPGKSAVGIE IPNSDREIVA LGDVLRSPVS SNDTHPMLIA
LGKDVEGSFL CANLAKMPHL LVAGATGAGK SSMINSLVVS VLMRATPDEV RMVLIDPKRV
ELTNYEGVPH LIAPIITNPK KAADVLSWVV REMEMRYDDL SVFGFRHIDD FNKAVKAGKV
NPPAGSDRVL EPYPYLLVIV DELADLMMVA AREVEESIVR ITQLARAAGI HLVLATQRPS
VDIVTGLIKA NVPSRLSFAT SSLADSRVIL DTPGAEKLVG QGDGLFLPMG ASKPVRIQGA
YISEREIEAV VNHVKSQLQP VYRIDLNAPI KSNVITDDVG DDLDLLLQAI QLVVSTQFGS
TSMLQRKLRI GFAKAGRLMD LMESRGIVGP TEGSKARAVL INAEQMPDVL ESIQGN
//
