FTSK_STAAM
ID FTSK_STAAM Reviewed; 788 AA.
AC P64164; Q99UJ6;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=SAV1276;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000017; BAB57438.1; -; Genomic_DNA.
DR RefSeq; WP_000035746.1; NC_002758.2.
DR AlphaFoldDB; P64164; -.
DR SMR; P64164; -.
DR PaxDb; P64164; -.
DR PRIDE; P64164; -.
DR EnsemblBacteria; BAB57438; BAB57438; SAV1276.
DR KEGG; sav:SAV1276; -.
DR HOGENOM; CLU_001981_9_2_9; -.
DR OMA; FVICIND; -.
DR PhylomeDB; P64164; -.
DR Proteomes; UP000002481; 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; 1.
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 Transmembrane; Transmembrane helix.
FT CHAIN 1..788
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098294"
FT TRANSMEM 34..54
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..788
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 453..649
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 209..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 209..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 788 AA; 88008 MW; 5DB54951FCC51FF0 CRC64;
MAQAKKKSTA KKKTASKKRT NSRKKKNDNP IRYVIAILVV VLMVLGVFQL GIIGRLIDSF
FNYLFGYSRY LTYILVLLAT GFITYSKRIP KTRRTAGSIV LQIALLFVSQ LVFHFNSGIK
AEREPVLSYV YQSYQHSHFP NFGGGVLGFY LLELSVPLIS LFGVCIITIL LLCSSVILLT
NHQHRDVAKV ALENIKAWFG SFNEKMSERN QEKQLKREEK ARLKEEQKAR QNEQPQIKDV
SDFTEVPQER DIPIYGHTEN ESKSQCQPSR KKRVFDAENS SNNIVNHQAD QQEQLTEQTH
NSVESENTIE EAGEVTNVSY VVPPLTLLNQ PAKQKATSKA EVQRKGQVLE NTLKDFGVNA
KVTQIKIGPA VTQYEIQPAQ GVKVSKIVNL HNDIALALAA KDVRIEAPIP GRSAVGIEVP
NEKISLVSLK EVLDEKFPSN NKLEVGLGRD ISGDPITVPL NEMPHLLVAG STGSGKSVCI
NGIITSILLN AKPHEVKLML IDPKMVELNV YNGIPHLLIP VVTNPHKAAQ ALEKIVAEME
RRYDLFQHSS TRNIKGYNEL IRKQNQELDE KQPELPYIVV IVDELADLMM VAGKEVENAI
QRITQMARAA GIHLIVATQR PSVDVITGII KNNIPSRIAF AVSSQTDSRT IIGTGGAEKL
LGKGDMLYVG NGDSSQTRIQ GAFLSDQEVQ DVVNYVVEQQ QANYVKEMEP DAPVDKSEMK
SEDALYDEAY LFVVEQQKAS TSLLQRQFRI GYNRASRLMD DLERNQVIGP QKGSKPRQVL
IDLNNDEV
