FTSK_CHLTR
ID FTSK_CHLTR Reviewed; 799 AA.
AC O84744;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=CT_739;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
RN [2]
RP INDUCTION.
RX PubMed=11532140; DOI=10.1046/j.1365-2958.2001.02550.x;
RA Gerard H.C., Krausse-Opatz B., Wang Z., Rudy D., Rao J.P., Zeidler H.,
RA Schumacher H.R., Whittum-Hudson J.A., Koehler L., Hudson A.P.;
RT "Expression of Chlamydia trachomatis genes encoding products required for
RT DNA synthesis and cell division during active versus persistent
RT infection.";
RL Mol. Microbiol. 41:731-741(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 inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}. Note=Located at the septum.
CC {ECO:0000250}.
CC -!- INDUCTION: During persistent infection, while it is induced one day
CC after infection, but transcription, it is severely down-regulated.
CC {ECO:0000269|PubMed:11532140}.
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; AE001273; AAC68334.1; -; Genomic_DNA.
DR PIR; B71478; B71478.
DR RefSeq; NP_220258.1; NC_000117.1.
DR RefSeq; WP_009872116.1; NC_000117.1.
DR AlphaFoldDB; O84744; -.
DR SMR; O84744; -.
DR STRING; 813.O172_04080; -.
DR EnsemblBacteria; AAC68334; AAC68334; CT_739.
DR GeneID; 884529; -.
DR KEGG; ctr:CT_739; -.
DR PATRIC; fig|272561.5.peg.812; -.
DR HOGENOM; CLU_001981_9_7_0; -.
DR InParanoid; O84744; -.
DR OMA; LCSRFPT; -.
DR Proteomes; UP000000431; 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; 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; SSF46785; SSF46785; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50901; FTSK; 1.
PE 2: Evidence at transcript level;
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_0000098250"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..799
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 460..659
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 274..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..485
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 799 AA; 87910 MW; 6DEB3326FABD5BE5 CRC64;
MGKERKKASV SLSPQTVFAV KTCVYLALAC FSGLSLWSFQ HNQPYTQNWI GLLGWSLSSF
LLYNFGVAAF LIPLNFGWLS FLNMKRTPAP LAFRKAAAFG AIPVCCAVLL SMISPAQNLP
QFLATRVPMV VMDLQPPKAY LGGIPFYLLY DGNSFSLKLL IGAVGTGLIF LAILLCAIFY
LIPKSFVLKK KALLDDLLKF LKNKFYACWN ACKKLLKNLV NNKSYVPKPS LRVPSSPSVA
KKEMLKLPTP VISLPLENKD LHDDSSVNRT IFLTPPHPTK RTLSPQKRTD LPNLLPKDSA
LAPAQTSYKP LPTPSPFVLA GDAPDLPQYH LLSKRNVHRP ESLLEELKKK AAILQQTLAS
FGIEAAIGNI CSGPTLAAFE VLPNTGVKVQ KIKALENDIA LNLQASSIRI IAPIPGKAAV
GIEIPNPDPQ PVNFRDLLED YQKGTQRLQV PLLLGKKANG DNFWTDLATM PHLIIAGTTG
SGKSVCINTI VMSLIMTSPP TDIKLVIVDP KKVELTGYSQ LPHMLTPVIT ESKEAHSALI
WLVREMELRY EILRFLGLRN IQSFNSRTRN VDIEASYDKE ISEKMPFIVG IIDELSDLLL
SSSHDIETPI VRLAQMARAV GIHLILATQR PSRDVITGLI KANFPSRIAF KVANKVNSQI
IIDEPGAENL MGNGDMLVVS PGSFAPVRVQ GAYICDDDIN KVIKDLCSRF PCKYVIPSFN
TYDDPGSMDP EDLDPLFNQA KTLVLQTGNA STTFLQRKLK IGYARAASII DQLEEARIVG
PSEGAKPRQI LVQLSNQDD
