ID A0A0Q8C9Q8_9MICO Unreviewed; 981 AA.
AC A0A0Q8C9Q8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KRA10922.1};
GN ORFNames=ASD61_01920 {ECO:0000313|EMBL:KRA10922.1};
OS Leifsonia sp. Root60.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736567 {ECO:0000313|EMBL:KRA10922.1, ECO:0000313|Proteomes:UP000051073};
RN [1] {ECO:0000313|EMBL:KRA10922.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA10922.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRA10922.1, ECO:0000313|Proteomes:UP000051073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root60 {ECO:0000313|EMBL:KRA10922.1,
RC ECO:0000313|Proteomes:UP000051073};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRA10922.1}.
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DR EMBL; LMGR01000001; KRA10922.1; -; Genomic_DNA.
DR RefSeq; WP_055817870.1; NZ_LMGR01000001.1.
DR AlphaFoldDB; A0A0Q8C9Q8; -.
DR STRING; 1736567.ASD61_01920; -.
DR Proteomes; UP000051073; 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: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; 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; 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:KRA10922.1};
KW Cell division {ECO:0000313|EMBL:KRA10922.1};
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:UP000051073};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 124..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 160..179
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..230
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 562..763
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 282..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 910..981
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..942
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 580..587
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 981 AA; 103601 MW; 6660833927A4E33B CRC64;
MATSTKATGR ARATPSSRGG AAKPPAKTPA KTPTKATPRA ASKTSAQTLK FTEVEEKPNL
LVRAWMGLAH VAGGAARALG PEQLAKEERR DGLPFFIILL AIAGAVFEWF LINDPVAQTL
DAWTFGGLVG RVAFALPIIM LVFAVWLFRH PSSVHDNSRI GIGLGILLVS IAGLCHVFGG
QPAPSDGMNV LARAGGILGW MITWPMMLVA PWLAVVVMIV LIALSLLIIT KTPPNRIPQR
MRELYAWLFG AHLPDEDERD EARLAAKAAK KERSQAVELD GIDGLGLDGD DEASTPDNLP
WWRRNTSGRE EDPAFEAAGV DGLTDVFGGA PEGAFDSALD GVGDGADAPP ARGGVTGDHY
GTEVMADLQA AEDAVKRFTG EVGGATTLLA DGAAVPDAAP GVLPGFSAAG AVFDQAGVAP
VDDQPTAPYH LPAASTLAAG APAKTRSAAN DEVVRAITDV LQQFSVDARV TGFSRGPTVT
QYEVELGPGV KVERVTALSK NLSYAVASNE VRILSPIPGK SAIGIEIPNS DREIVTLGDV
LRSGAAAKST HPMTIGVGKD VGGGFVLANL AKMPHLLVAG STGSGKSSFV NSMITSLLMR
ATPADVRMVL IDPKRVELAP YAGVPHLITP IITNPKKAAE ALSWVVKEMD MRYDDLASFG
FRHIDDFNKA VINEEIILPA GSERQLKPYP YLLVVVDELA DLMMVAPRDV EDSIVRITQL
ARASGIHLVL ATQRPSVDVV TGLIKANVPS RLAFAVTSVT DSRVILDQPG ADKLIGQGDA
LFLPMGASKA LRVQGAWVSE SEIERVVKHV TRQARPEYRP DVAVSAERKA IDSDIGDDLE
LLLAAAELVV STQFGSTSML QRKLRVGFAK AGRLMDLLES REIVGPSEGS KARDVLVTAE
QLPGVLARLR GEDDGSAPSA ASVAPSAPQQ TTVQQGMQAG MQQTAAPVDP YGDDPVARMT
EGYPEEEGDS DEDAWNLTGR D
//
