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FTSK_CALS4
ID   FTSK_CALS4              Reviewed;         709 AA.
AC   Q8R5S4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=TTE1378;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(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; AE008691; AAM24600.1; -; Genomic_DNA.
DR   RefSeq; WP_011025666.1; NC_003869.1.
DR   AlphaFoldDB; Q8R5S4; -.
DR   SMR; Q8R5S4; -.
DR   STRING; 273068.TTE1378; -.
DR   EnsemblBacteria; AAM24600; AAM24600; TTE1378.
DR   KEGG; tte:TTE1378; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_2_9; -.
DR   OMA; NEMTERY; -.
DR   OrthoDB; 349533at2; -.
DR   Proteomes; UP000000555; 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; IPR025199; FtsK_4TM.
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; PF13491; FtsK_4TM; 1.
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..709
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098312"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        48..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        158..709
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          376..563
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         396..401
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   709 AA;  78916 MW;  BC76C0B84F0A4E7F CRC64;
     MIDKKQKPVK EEIVGIIFLA FTLISFLSLY TDSTGIIGKH IGIFLKGFFG TGSYVISALL
     LVFALMFLFT NKNFIKLHRS MALLGLFLMF ISLNQLYYFP VLTDFKDYLS VAYISGINNT
     GGGIIGSLIV YFLVKMVGII GSYILLISFT AIFIVLITDI SLVSLIKSSY DKLKDRKKVS
     AKNKLQDKMA EKKAEEVEST EELVEVEKKE RIDVPIEIVE QVEEERKVYE KAFLEKEEGE
     YTPPPITLLK EAIPSPKIKN EVLLEKAKKI EETLRNFGIE AKVVQVTKGP AITRFELQPS
     AGVKVSRIVS LTDDLALSLA APSVRIEAPI PGKSAIGIEV PNEKITPVYL REVIDSKKFR
     SFKSELAIGL GKDIAGNIVI ADLAKMPHLL IAGATGSGKS VCINSLIVSL LYKASPKQVK
     MILIDPKVVE LNIYNGIPHL LTPVVTDPKK AAGVLNWAVQ EMIRRYSLFA DHGVRDIESY
     NEKYKEERLY KIVIIIDELS DLMMVSPAEV EEYIFRLAQM ARAAGIHLVI ATQRPSVDVI
     TGVIKANIPS RISFAVSSQI DSRTILDMTG AEKLLGKGDM LFDPIGASKP IRVQGAFISE
     EEVEAVVNFL KENYSSHYEE IKVEEKTNGK NLDEEEDELL EDAVSVILET GQASISLLQR
     KLRIGYARAA RIIDQLEQKG IISGYDGAKP RQIILPREEI QKILERKSV
 
 
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