ID A0A0C1UAP1_9ACTN Unreviewed; 803 AA.
AC A0A0C1UAP1;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=FtsK domain-containing protein {ECO:0000259|PROSITE:PS50901};
GN ORFNames=MB53_05140 {ECO:0000313|EMBL:KIE49854.1};
OS marine actinobacterium MedAcidi-G2A.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1550400 {ECO:0000313|EMBL:KIE49854.1, ECO:0000313|Proteomes:UP000031257};
RN [1] {ECO:0000313|EMBL:KIE49854.1, ECO:0000313|Proteomes:UP000031257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL Submitted (SEP-2014) 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:KIE49854.1}.
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DR EMBL; JUEN01000023; KIE49854.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1UAP1; -.
DR STRING; 1550400.MB53_05140; -.
DR Proteomes; UP000031257; 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 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};
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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 51..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 431..637
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 209..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..726
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 774..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..718
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 448..455
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 803 AA; 85621 MW; 9760E729C808DEC8 CRC64;
MIGIAGRTFR SAFSGHKADL ISLGLIVIGL VAALGLYFGT AGIVGKAIGP WVFRSIFGFV
GYLAPAALIA AGIYLTFEVP EEDESSSPKD NSSRFAPLSI GSLFIFSAIC GLSHLNTDAG
SYGLSSIGEL KKGGGALGYL VGSPLRAAFE QIGATFVLIA IGLVGVIVIT GMTFRESLSK
TWLLLRGIYR AIANTIFLAM GETKEEIAQR KGSSEAPLIQ IDGESRPVGK GKKESKKLKS
EASSDSSDKN MSQENKDDAT ESDNKSKSLI SSKAEDPVIS GEQLEIELGP AAKGSVWKLP
SDKILVRSAS QDINEKLVEE RGRVLERALA AHGVETRLVG MVVGPTVTRY ELELGAGVKV
SRVTTLNKDI AYAMASADVR ILAPIPGRQA IGVEVPNNER QVVALGDVLS SVEAQRATHP
LEVAIGRDIN GKSIVMNLSE MPHILIAGAT GAGKSSCINS IVTSALMRST PETLRMILID
PKRVEMSQYE RVPHLLTQPV VDPKKAANAL QWACREMDRR YELLAEVRFR DIAGYNAAYD
KGSIEAPPSA INPDGSPKTY SRLPFILVVV DELSDLMMVA PRDVEDSICR IAQKARAVGI
HLVVATQRPS TNVITGVIKA NIPARIAFAV SSLTDSRVIL DQGGAERLVG QGDMLLLDPK
SSSPHRIQGA WVSEDEVKRV VGAWRKQADQ LKGKGKVDEI STQQSITEQP TSASAEGLPG
GTTGDAGDDE LLLKAIELVV DSQLGSTSML QRKLRVGFAR AGRIMDLLED RGIVGPSEGS
KPREVLMTAE QISDQKSAGE GPV
//
