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FTSK_TREPA
ID   FTSK_TREPA              Reviewed;         799 AA.
AC   O83964;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=TP_0999;
OS   Treponema pallidum (strain Nichols).
OC   Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX   NCBI_TaxID=243276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nichols;
RX   PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA   Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA   Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA   Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA   Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA   McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA   Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA   Venter J.C.;
RT   "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL   Science 281:375-388(1998).
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 inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=Located at the septum.
CC       {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; AE000520; AAC26587.1; -; Genomic_DNA.
DR   PIR; H71255; H71255.
DR   RefSeq; WP_010882443.1; NC_021490.2.
DR   AlphaFoldDB; O83964; -.
DR   SMR; O83964; -.
DR   STRING; 243276.TPANIC_0999; -.
DR   EnsemblBacteria; AAC26587; AAC26587; TP_0999.
DR   GeneID; 57879510; -.
DR   KEGG; tpa:TP_0999; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_11_2_12; -.
DR   OMA; IYGEKCY; -.
DR   OrthoDB; 349533at2; -.
DR   Proteomes; UP000000811; 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 inner membrane; Cell membrane;
KW   Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..799
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098313"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        55..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        124..144
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        145..799
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          470..662
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          167..208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         490..495
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   799 AA;  86606 MW;  009E39B56A82DE67 CRC64;
     MERSPLPRII ALTFGTLLFV SAVLLTLSTF LPLFTLHRAS HWFFVPGTLL YETYAFSSLL
     VPLLLLHTAL LLFVGGRSLR AESALVAFPL LFITAVCGEH GLYALRRALA ARSISPSTRG
     GIDIVCVLCL LALLGAELYA ALIYGERCYV WFHARIPRDF IADGFQDPSF PPSTADHPDT
     VSPPPAPSCA TADVQTPEAS APPEGQFSTE VPLQGGEFLI SEAEVQPATQ VAACGGVSTP
     TALAPSVPSQ APFPLLPAPG LIQSNLPSDV HAPASPGSLP SVIPAQAPCV MALSPISAPS
     VAPAETLIPA QDDEQGPPRP IPASAAPLRH PCRGYQVPYD LLDQYSEDTY EGIDELTKNL
     ALLLEETFSE FNIRVEITGI KKGPVVTMFE LLPPPGIKLS KITNLQDNVA LKLAASSVRI
     VAPIPGKHAI GVEVPNKKRS LVTFKELLHT RTAGSNRMAI PVILGKDVTG EPQVIDLAQT
     PHLLIAGATG SGKSVCVNAL ILSILYHKCP DETKLLLIDP KIVELKLYND IAHLLTPVIT
     EPKRALQALQ YILCEMERRY ALLEQLECRD IKTYNKKIQE KSIATQPLPF IVIIIDEFAD
     LMVASGKELE TSVARLCAMS RAVGIHLVLA TQRPSIDVIT GLIKANIPSR IAFMVSSKMD
     SRIILDEMGA EKLLGRGDML YMNPSQSFPT RIQGAYVSER ELARVIAHVR AWGTPEYLDE
     EIFFDDDDAS ISGNFVDESD PLYEQAVQVV QYAGKASTSY VQRKLKIGYN RAARLIEEME
     ARGVVGPPNG SKPRDVLRS
 
 
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