FTSK_CHLMU
ID FTSK_CHLMU Reviewed; 794 AA.
AC Q9PLI7;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=DNA translocase FtsK;
GN Name=ftsK; OrderedLocusNames=TC_0112;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
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; AE002160; AAF38991.1; -; Genomic_DNA.
DR PIR; A81741; A81741.
DR RefSeq; WP_010229403.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PLI7; -.
DR SMR; Q9PLI7; -.
DR STRING; 243161.TC_0112; -.
DR EnsemblBacteria; AAF38991; AAF38991; TC_0112.
DR GeneID; 1245642; -.
DR KEGG; cmu:TC_0112; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_7_0; -.
DR OMA; LCSRFPT; -.
DR OrthoDB; 349533at2; -.
DR Proteomes; UP000000800; 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 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 Transmembrane; Transmembrane helix.
FT CHAIN 1..794
FT /note="DNA translocase FtsK"
FT /id="PRO_0000098247"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 59..79
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..794
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 455..654
FT /note="FtsK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT REGION 265..311
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 475..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 794 AA; 87316 MW; 6A10CA3E2CFF6E10 CRC64;
MRKERKKASV SLSPQTVFAI KTCIYLALAC FSGLSLWSFQ HNQPYTQNWI GLLGWSLSSF
LLYNFGVAAF LIPLYFGFLS FLNMKKTPAP LAFRKAVAFG TVPVCCAILL SMVSPAQNLP
QFLATRVPMV VMDLQPPKAY LGGIPFYLLY DGNSFSLKLL IGAVGTGLIF LAILLCAICY
LIPKSFVLKK KALLDALLKF LKNKSYACWS ACKKLLKNLV NNKSYCPEPS LRVPAPSSFA
KKEVLKLPTP VISLPLENKD LHDGDSSNRT IFLSPPHPAK RTLAPQKKPD LPDLLQKRTS
STPIPSSSPS PFIVAGEAPD LPQYHLLSKR NIRRPESLLE ELKKKAAILQ QTLASFGIDA
SIGNICSGPT LAAFEVLPNT GVKVQKIKAL ENDIALNLQA SSIRIIAPIP GKAAVGIEIP
NPDPQPVNFR DLLEDYQKGT QRLQVPLLLG KKANGDNFWT DLATMPHLII AGTTGSGKSV
CINTIVMSLI MTSPPTDVKL VIVDPKKVEL TGYSQLPHML TPVITESKEA HSALIWLVRE
MELRYEILRF LGLRNIQSFN SRTRNVDIEA SYDKEIPEKM PFIVGIIDEL SDLLLSSSHD
IETPIVRLAQ MARAVGIHLI LATQRPSRDV ITGLIKANFP SRIAFKVANK VNSQIIIDEP
GAENLMGNGD MLVVSPGSFA PLRVQGAYIC DDDINKVIKD LCSRFPCKYV IPSFDTYDDS
SSMDPESLDP LFNQAKTLVL QTGNASTTFL QRKLKIGYAR AASIIDQLEE ARIVGPSEGA
KPRQILVQLS NQED
