FTSK_STAEQ
ID FTSK_STAEQ Reviewed; 797 AA.
AC Q5HPR5;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=SERP0843;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(2005).
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; CP000029; AAW54212.1; -; Genomic_DNA.
DR RefSeq; WP_002439534.1; NC_002976.3.
DR AlphaFoldDB; Q5HPR5; -.
DR SMR; Q5HPR5; -.
DR STRING; 176279.SERP0843; -.
DR PRIDE; Q5HPR5; -.
DR EnsemblBacteria; AAW54212; AAW54212; SERP0843.
DR GeneID; 50018912; -.
DR KEGG; ser:SERP0843; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_2_9; -.
DR OMA; FVICIND; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000000531; 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; IPR036259; MFS_trans_sf.
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; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00843; Ftsk_gamma; 1.
DR SUPFAM; SSF103473; SSF103473; 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..797
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098300"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 92..112
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 172..797
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 462..658
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 199..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482..487
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 797 AA; 89453 MW; B477E3828C7C0E1A CRC64;
MPQAKKRTST KRKGNKKTNK KKQNETPLRY IFSIIVVILI ILGAFQLGII GRMIDSFFNY
LFGMSRYLTY ILVLIATIFI TYSKQIPRTR RSIGAIVLQL ALLFIAQLYF HFSHNITSQR
EPVLSFVYKA YEQTHFPNFG GGLIGFYLLK LFIPLISIVG VIIITILLLA SSFILLLNLR
HRDVTKSLFD NLKSSSNHAS ESIKQKREQN KIKKEEKAQL KEAKIERKKQ KKSRQNNNVI
KDVSDFPEIS QSDDIPIYGH NEQEDKRPNT ANQRQKRVLD NEQFQQSLPS TKNQSINNNQ
PSTTAENNQQ QSQAEGSISE AGEEANIEYT VPPLSLLKQP TKQKTTSKAE VQRKGQVLES
TLKNFGVNAK VTQIKIGPAV TQYEIQPAQG VKVSKIVNLH NDIALALAAK DVRIEAPIPG
RSAVGIEVPN DKISLVTLKE VLEDKFPSKY KLEVGIGRDI SGDPISIQLN EMPHLLVAGS
TGSGKSVCIN GIITSILLNT KPHEVKLMLI DPKMVELNVY NGIPHLLIPV VTNPHKASQA
LEKIVSEMER RYDLFQHSST RNIEGYNQYI RKQNEELDEK QPELPYIVVI VDELADLMMV
AGKEVENAIQ RITQMARAAG IHLIVATQRP SVDVITGIIK NNIPSRIAFA VSSQTDSRTI
IGAGGAEKLL GKGDMLYVGN GESTTTRIQG AFLSDQEVQD VVNYVVEQQK ANYVKEMEPD
APVDKSEMKS EDALYDEAYL FVIEKQKAST SLLQRQFRIG YNRASRLMDD LERNQVIGPQ
KGSKPRQILV DLENDEV
