ID   FTSK_PSEPK              Reviewed;         834 AA.
AC   Q88FS8;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=PP_4004;
OS   Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS   / KT2440).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=160488;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX   PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA   Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA   Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA   Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA   Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA   Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA   Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA   Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA   Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT   "Complete genome sequence and comparative analysis of the metabolically
RT   versatile Pseudomonas putida KT2440.";
RL   Environ. Microbiol. 4:799-808(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. Translocation stops specifically at Xer-dif sites, where FtsK
CC       interacts with the Xer recombinase, allowing activation of chromosome
CC       unlinking by recombination. FtsK orienting polar sequences (KOPS) guide
CC       the direction of DNA translocation. FtsK can remove proteins from DNA
CC       as it translocates, but translocation stops specifically at XerCD-dif
CC       site, thereby preventing removal of XerC and XerD from dif (By
CC       similarity). {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 multimerise to produce a hexameric ring,
CC       contain the nucleotide binding motif and form the DNA pump. The gamma
CC       subdomain is a regulatory subdomain that controls translocation of DNA
CC       by recognition of KOPS motifs and interacts with XerD recombinase (By
CC       similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN69598.1; -; Genomic_DNA.
DR   RefSeq; NP_746134.1; NC_002947.4.
DR   RefSeq; WP_010954811.1; NC_002947.4.
DR   AlphaFoldDB; Q88FS8; -.
DR   SMR; Q88FS8; -.
DR   STRING; 160488.PP_4004; -.
DR   EnsemblBacteria; AAN69598; AAN69598; PP_4004.
DR   KEGG; ppu:PP_4004; -.
DR   PATRIC; fig|160488.4.peg.4260; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_7_6; -.
DR   OMA; YKAEARD; -.
DR   PhylomeDB; Q88FS8; -.
DR   BioCyc; PPUT160488:G1G01-4271-MON; -.
DR   Proteomes; UP000000556; 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; 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; 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..834
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098279"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        73..93
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        168..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        189..834
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          473..685
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          238..318
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         493..498
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   834 AA;  91296 MW;  B45B0768A999BAFC CRC64;
     MKKSTATPAP LPVPLWRQQL HYRLKEGALI AVGALCLYLW MALLTYDTSD PGFSHTSNVD
     QVQNAAGRAG AYFADILFMV LGYFAYIFPL LLAVKTWQIF RERHQPWDWS GWLFSWRLIG
     LVFLVLSGAA LAHIHFHPPA SLPFSAGGAL GESLGDLARN LLNVQGSTLM FIALFLFGLT
     VFTDLSWFKV MDLTGKITLD LFELVQGAAT RWWEARNERK RLEAQLREDE PVFKAAPMAA
     EKREPAKPSL RERILKREEP PAQPVEPREP TLAREPIVPP RETAPEALAP RETVVPRQQH
     AAPTIVPPSA ASRAPEPSKR AMKEKQAPLF VDSAVEGTLP SISILDPAEQ KKIEYSPESL
     AGVGQLLEIK LKEFGVEVAV DSIHPGPVIT RYEIQPAAGV KVSRIANLAK DLARSLAVTS
     VRVVEVIPGK TTVGIEIPNE NRQMVRFSEV LATPQYDEQK SPVTLALGHD IGGKPVITDL
     AKMPHLLVAG TTGSGKSVGV NAMILSILFK SSPEDARLIM IDPKMLELSI YEGIPHLLCP
     VVTDMKDAAN ALRWSVAEME RRYKLMAAMG VRNLAGFNRK IKDAQEAGEV IHDPLYRRES
     MDDEPPALKT LPTIVVVVDE FADMMMIVGK KVEELIARIA QKARAAGIHL ILATQRPSVD
     VITGLIKANI PTRMAFQVSS KIDSRTIIDQ GGAEQLLGHG DMLYMPPGTS LPIRVHGAFV
     SDDEVHRTVE AWKLRGAPDY NDDILNGVEE AGSGFDGGGG GGEGDDAETD ALYDEAVQFV
     LESRRASISA VQRKLKIGYN RAARMIESME MAGVVTPMNS NGSREVIAPG GPRD