ID A0A0X3XX19_9ACTN Unreviewed; 933 AA.
AC A0A0X3XX19;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KUL79030.1};
GN ORFNames=ADL34_05695 {ECO:0000313|EMBL:KUL79030.1};
OS Streptomyces sp. NRRL WC-3605.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL79030.1, ECO:0000313|Proteomes:UP000052945};
RN [1] {ECO:0000313|EMBL:KUL79030.1, ECO:0000313|Proteomes:UP000052945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL79030.1,
RC ECO:0000313|Proteomes:UP000052945};
RA Gilbert D.G.;
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 -!- 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:KUL79030.1}.
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DR EMBL; LLZN01000035; KUL79030.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X3XX19; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000052945; 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:KUL79030.1};
KW Cell division {ECO:0000313|EMBL:KUL79030.1};
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:UP000052945};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 116..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 146..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..202
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..261
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 582..782
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 381..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..339
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 599..606
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 933 AA; 99299 MW; 7404D825388A27E1 CRC64;
MKQWAHVSTV TSTGNLTSMA SRSSAAKKPP AKKAAAPAKA PAKKAAARKA PAKKAPAKKA
AARRAAPPPK PAPSPTGGVY RFVRAIWLGL AHAVGAVFRG IGQGAKNLDP AHRKDGVALL
LLGLSLIVAA GTWSNLRGPV GDLVEIIVTG AFGRLDLLVP ILLAVIAVRF IRHPEKPEAN
GRIVIGLSAL AVGVLGQVHI AVGSPARSAG MQAIRDAGGL IGWGAATPLT YTMGEVLAVP
LLVLLTVFGL LVVTATPVNA IPQRLRLLGV KLGLLPDPED DEDYTEDDER YDEQWRESLP
AARGRKRGRP REAYDPEDAE QEALSRRRGR PRRSAVPQPE MDRPMDAVDV AAAAAAALDG
AVMHGMPPSP IVADLTQGVS VGDREDTTPV PTPVPAARPQ QDRLPRAKAA DLTKTEVPDL
TKAAPVPDEI RDLPPRAEQL QLSGDITYAL PSLDLLERGG PGKSRSAAND AVVASLTTVF
TEFKVDARVT GFTRGPTVTR YEVELGPAVK VERITALTKN IAYAVASPDV RIISPIPGKS
AVGIEIPNTD REMVNLGDVL RLAAAAEDDH PMLVALGKDV EGGYVMANIA KMPHVLVAGA
TGSGKSSCIN CLITSIMMRA TPEDVRMVLV DPKRVELTAY EGIPHLITPI ITNPKRAAEA
LQWVVREMDL RYDDLAAYGY RHIDDFNEAV RSGKVKAPEG SERELQPYPY LLVIVDELAD
LMMVAPRDVE DAIVRITQLA RAAGIHLVLA TQRPSVDVVT GLIKANVPSR LAFATSSLAD
SRVILDQPGA EKLIGKGDGL FLPMGANKPT RMQGAFVTED EVAAVVQHCK DQMAPVFRDD
VVVGTKQKKE IDEEIGDDLD LLCQAAELVV STQFGSTSML QRKLRVGFAK AGRLMDLMES
RGVVGPSEGS KARDVLVKAD ELDGVLAVIR GEA
//
