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FTSK_STRMU
ID   FTSK_STRMU              Reviewed;         787 AA.
AC   Q8DSX7;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=SMU_1629c;
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159;
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA   Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(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 difSL
CC       recombination site, which is located within the replication terminus
CC       region. Required for activation of the XerS 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   -!- SEQUENCE CAUTION:
CC       Sequence=AAN59270.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014133; AAN59270.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_721964.1; NC_004350.2.
DR   RefSeq; WP_002352345.1; NC_004350.2.
DR   AlphaFoldDB; Q8DSX7; -.
DR   SMR; Q8DSX7; -.
DR   STRING; 210007.SMU_1629c; -.
DR   PRIDE; Q8DSX7; -.
DR   EnsemblBacteria; AAN59270; AAN59270; SMU_1629c.
DR   KEGG; smu:SMU_1629c; -.
DR   PATRIC; fig|210007.7.peg.1452; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_6_9; -.
DR   OMA; MTKEPEI; -.
DR   Proteomes; UP000002512; 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..787
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098305"
FT   TRANSMEM        31..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        92..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        184..787
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          450..647
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          279..303
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          702..729
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         471..476
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   787 AA;  87176 MW;  BAD7C3C0BCF3D464 CRC64;
     MAKTKNKRKG RKTRRPTKAE LEKQRAIKRM VFALFMAFVL FFAIFKLGRV GVTVYNIIRL
     MVGSLAYPFI FAALIYLFAT KWLKKHDGLV GGFVITMLGM LLEWQAYLFS LATMKDQSVI
     KGTLVIVFSD LSKFRVANFA GGGFLGALLY MPVAFLFSNI GSFLIGGLFL LLGLFLMSPW
     DVYDVMNFFK DSYAKWQVKR QENREKRFAQ KEEARLLAQQ AVQEAQESAT FDHGLNAAID
     LETGEVLDQA QTIDLDDFDG QVHKEPEIIG YQSDPEGEAL EAEVPAAEQT SQLPKEEDMS
     DESLEVDFTP KTTLHYKLPG IDLFAKDKPK NQSKEKRLVR DNIKILEETF TSFGIKANVE
     RAEIGPSVTK YEVKPAVGVR VNRISNLADD LALALAAQDV RIEAPIPGKS LVGIEVPNSE
     VATVTFRELW EQAKASPDKL LEVPLGKAVN GSVRSFDLAK MPHILVAGST GSGKSVAVNG
     IIASILMKAR PDQIKFMMID PKMVELSVYN DIPHLLIPVV TNPRKASKAL QKVVDEMENR
     YELFSHFGVR NIAGYNAKVE EFNRHSETKH IPLPLLVVIV DELADLMMVA SKEVEDAIIR
     LGQKARAAGI HMILATQRPS VDVISGLIKA NVPSRIAFAV SSGTDSRTIL DENGAEKLLG
     RGDMLFKPID ENHPVRLQGS FISDDDVERI VSFIKEQAEA DYDESFDPGE VSEDDNSNGN
     GGNSEGDPLF EDAKALVLET QKASASMLQR RLSVGFNRAT RLMEELEEAG VIGPAEGTKP
     RKVLQSN
 
 
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