ID A0A2T7SMT9_9ACTN Unreviewed; 963 AA.
AC A0A2T7SMT9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:PVE04210.1};
GN ORFNames=Y717_12660 {ECO:0000313|EMBL:PVE04210.1};
OS Streptomyces scopuliridis RB72.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE04210.1, ECO:0000313|Proteomes:UP000245992};
RN [1] {ECO:0000313|EMBL:PVE04210.1, ECO:0000313|Proteomes:UP000245992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB72 {ECO:0000313|EMBL:PVE04210.1,
RC ECO:0000313|Proteomes:UP000245992};
RA Olson J.B.;
RT "Annotated genome of Streptomyces scopuliridis.";
RL Submitted (DEC-2013) 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:PVE04210.1}.
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DR EMBL; AZSP01000392; PVE04210.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7SMT9; -.
DR STRING; 1440053.GCA_000718095_00896; -.
DR Proteomes; UP000245992; 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:PVE04210.1};
KW Cell division {ECO:0000313|EMBL:PVE04210.1};
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:UP000245992};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..177
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..207
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 610..810
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..25
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..65
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 627..634
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 963 AA; 101888 MW; 194025D8D2C9529B CRC64;
MSPAVHTGNL TIMASSTSGK GSQGTAGTAK PRAGRTTGAA KAAPAKKTAA KKSAPAKKAP
VKKAPAKKAA AKAAPKPAPS PTGGVYRLVR AVWLGAAHGV GAMFRGIGRG AKGLDPAHRK
DGLALLLLGL ALIVAAGTWS NLRGPVGDLV EMLITGAFGR LDLLVPILLG AIAVRLILYP
EKPEANGRIV IGLSALVIGV LGLVHVACGA PGRGAGTEAI QDAGGLIGWA ASTPLIFTTG
EVLAVPLLLL LTIFGLLVVT ATPVNAIPQR LRLLGTKLGI IQPDRDPERF DDFDDDERYD
DDERYDEQWR EALPSGGRRP GTRRRGSPAE YDPDRAEVEA LSKRRRPRRA SVQPSMDRPM
DAVDVAAAAA AALDGAVLNG MPPSPIVADL TQSVSVERGR KPGQPPGERQ EPLEEPAEDA
AERSVPGSVP LPTAREAERP RAGTAGVADL TKPPPERDKP LPPRAEQLQL RGDITYSLPS
LDLLERGGPG KTRSAANDAV VASLSNVFME FKVDAAVTGF TRGPTVTRYE VELGPAVKVE
RITALTKNIA YAVASPDVRI ISPIPGKSAV GIEIPNTDRE MVNLGDVLRL ADAAEDDHPM
LVALGKDVEG GYVMANLAKM PHVLVAGATG SGKSSCINCL ITSVMVRATP EDVRMVLVDP
KRVELTAYEG IPHLITPIIT NPKRAAEALQ WVVREMDLRY DDLAAYGYRH IDDFNKAVRD
GKARAPEGSE RELSPYPYLL VIVDELADLM MVAPRDVEDS IVRITQLARA AGIHLVLATQ
RPSVDVVTGL IKANVPSRLA FATSSLADSR VILDQPGAEK LIGKGDGLFL PMGANKPTRM
QGAFVTEDEV AAIVQHCKDQ MAPVFRDDVV VGTAKKKEID EDIGDDLDLL CQAAELVVST
QFGSTSMLQR KLRVGFAKAG RLMDLMESRN IVGPSEGSKA RDVLVKADEL DGVLAVICGE
SPS
//
