FTSK_STAAW
ID FTSK_STAAW Reviewed; 789 AA.
AC Q8NWY8;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=MW1159;
OS Staphylococcus aureus (strain MW2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=196620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MW2;
RX PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT "Genome and virulence determinants of high virulence community-acquired
RT MRSA.";
RL Lancet 359:1819-1827(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; BA000033; BAB95024.1; -; Genomic_DNA.
DR RefSeq; WP_000035773.1; NC_003923.1.
DR AlphaFoldDB; Q8NWY8; -.
DR SMR; Q8NWY8; -.
DR EnsemblBacteria; BAB95024; BAB95024; BAB95024.
DR KEGG; sam:MW1159; -.
DR HOGENOM; CLU_001981_9_2_9; -.
DR OMA; FVICIND; -.
DR Proteomes; UP000000418; 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..789
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098298"
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..789
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 454..650
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..275
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 474..479
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 789 AA; 88201 MW; C2F50DA04BCEB2C9 CRC64;
MAQAKKKSTA KKKTTSKKRT NSRKKKNDNP IRYVIAILVV VLMVLGVFQL GIIGRLIDSF
FNYLFGYSRY LTYILVLLAT GFITYSKRIP KTRRTAGSIV LQIALLFVSQ LVFHFNSGIK
AEREPVLSYV YQSYQHSHFP NFGGGVLGFY LLELSVPLIS LFGVCIITIL LLCSSVILLT
NHQHREVAKV VLENIKAWFG SFNEKMSERN QEKQLKREEK ARLKEEQKAR QNEQPQIKDV
SDFTEVPQER DIPIYGHTEN ESKSQSQPSR KKRVFDAENS SNNIVNHHQA DQQEQLTEQT
HNSVESENTI EEAGEVTNVS YVVPPLTLLN QPAKQKATSK AEVQRKGQVL ENTLKDFGVN
AKVTQIKIGP AVTQYEIQPA QGVKVSKIVN LHNDIALALA AKDVRIEAPI PGRSAVGIEV
PNEKISLVSL KEVLDEKFPS NNKLEVGLGR DISGDPITVP LNEMPHLLVA GSTGSGKSVC
INGIITSILL NAKPHEVKLM LIDPKMVELN VYNGIPHLLI PVVTNPHKAA QALEKIVAEM
ERRYDLFQHS STRNIKGYNE LIRKQNQELD EKQPELPYIV VIVDELADLM MVAGKEVENA
IQRITQMARA AGIHLIVATQ RPSVDVITGI IKNNIPSRIA FAVSSQTDSR TIIGTGGAEK
LLGKGDMLYV GNGDSSQTRI QGAFLSDQEV QDVVNYVVEQ QQANYVKEME PDAPVDKSEM
KSEDALYDEA YLFVVEQQKA STSLLQRQFR IGYNRASRLM DDLERNQVIG PQKGSKPRQV
LIDLNNDEV
