FTSK_CLOPE
ID FTSK_CLOPE Reviewed; 796 AA.
AC Q8XJS8;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=CPE1676;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}. Note=Located at the septum. {ECO:0000250}.
CC -!- DOMAIN: Consists of an N-terminal domain, which is sufficient for the
CC localization to the septal ring and is required for cell division,
CC followed by a linker domain, and a C-terminal domain, which forms the
CC translocation motor involved in chromosome segregation. The C-terminal
CC domain can be further subdivided into alpha, beta and gamma subdomains.
CC The alpha and beta subdomains form the DNA pump, and the gamma
CC subdomain is a regulatory subdomain (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR EMBL; BA000016; BAB81382.1; -; Genomic_DNA.
DR RefSeq; WP_003469176.1; NC_003366.1.
DR AlphaFoldDB; Q8XJS8; -.
DR SMR; Q8XJS8; -.
DR STRING; 195102.gene:10490940; -.
DR EnsemblBacteria; BAB81382; BAB81382; BAB81382.
DR KEGG; cpe:CPE1676; -.
DR HOGENOM; CLU_001981_9_2_9; -.
DR OMA; NEMTRRY; -.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF17854; FtsK_alpha; 1.
DR Pfam; PF09397; FtsK_gamma; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell membrane;
KW Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..796
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098252"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 93..113
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 177..796
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 458..649
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT BINDING 478..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 796 AA; 88367 MW; FF3C630F9D2DE783 CRC64;
MAGGKKKTAT KTQKKKNQSQ IKVTEEIYAL IAICVSLIVM FSLYTDKAGY LSVISRTLLI
GLFGIGAFFI PIYIIYLCTK LFLFKREVLF SRIGLGITIA LITSVLLIQT VNINDYYVQG
SIWGSIKTIW HSQSEWHGGV VGFLIVLPLY KLVGKIGLFV IFVTLYLISS MLIFDYNLVS
IRNFFGGFKE KASKVKFVDK KYEKDDYINL KKKDGASEGN KESKKDDISE DNNKIKILDF
MKNSSLNDIE DNKKEKDNQL KDNIKINDFK QESKMPRDLS LDNTIIEQRG FNSEKAKEEE
SIDKEISNNI ASKGSSVGAS YVAPNADLLN LNNNNELDKD DKKALLANAA KLEETLMSFG
VEAKILQVTK GPSVTRFELQ PKAGIKVSKI VNLADDIALG LAAKGVRIEA PIPGKSAIGI
EVPNKEQTPV FFREIVESKE FLDNKFKVAC ALGKDITGKA VVTDLSKMPH VLIAGATGSG
KSVCINTLIV SILYKYSPDE VKLLMIDPKV VELNVYNGIP HLLIPVVTDP KKAAAALNWA
VNEMTRRYKL FADNGVRNIE SYNALYNKGE VPEKLPYIVI IVDELADLMM ACPHDVEDYI
CRLAQMARAA GMHLVIATQR PSVDVITGVI KANIPSRISF AVSSQIDSRT ILDSAGAEKL
LGRGDMLFYP VGESKPQRVQ GAFISEEEVE HVVSFIKESQ RDAQYEEDIL EHINSATIAS
EGNGDGDRDE LLDEAIEIVV ESGQASASYL QRRLRIGFNR AARIIEELEE CGVISRRDGS
KPRQVLLSKD ELENMK
