ID   FTSK_COXBU              Reviewed;         778 AA.
AC   P39920;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   09-MAY-2003, sequence version 2.
DT   27-MAR-2024, entry version 135.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; Synonyms=spoIIIE; OrderedLocusNames=CBU_1191;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Nine Mile phase I / Bratislava;
RX   PubMed=8237209; DOI=10.1111/j.1439-0450.1993.tb00151.x;
RA   Oswald W., Thiele D.;
RT   "A sporulation gene in Coxiella burnetii?";
RL   J. Vet. Med. B 40:366-370(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO90700.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; X75627; CAA53289.1; -; Genomic_DNA.
DR   EMBL; AE016828; AAO90700.2; ALT_INIT; Genomic_DNA.
DR   PIR; S43132; S43132.
DR   RefSeq; NP_820186.2; NC_002971.3.
DR   AlphaFoldDB; P39920; -.
DR   SMR; P39920; -.
DR   STRING; 227377.CBU_1191; -.
DR   EnsemblBacteria; AAO90700; AAO90700; CBU_1191.
DR   GeneID; 1209095; -.
DR   KEGG; cbu:CBU_1191; -.
DR   PATRIC; fig|227377.7.peg.1189; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_9_7_6; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007059; P:chromosome segregation; IEA:UniProtKB-KW.
DR   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.30.980.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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..778
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098256"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        193..778
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          419..629
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         439..444
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   CONFLICT        64
FT                   /note="A -> P (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        79..80
FT                   /note="LY -> KN (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        87
FT                   /note="Y -> N (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        102
FT                   /note="R -> P (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        121
FT                   /note="A -> P (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        159
FT                   /note="A -> P (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="T -> A (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="F -> C (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200
FT                   /note="K -> R (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        236
FT                   /note="T -> A (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="P -> R (in Ref. 1; CAA53289)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   778 AA;  85251 MW;  54B9D88081D73F7D CRC64;
     MGRRKGKKSA KETGVLLRRH LRYRLREGCF ILALAFSAFL FIALLSYHRS DPGWSHSIVV
     KHVANLTGEA GAWLSDFTLY MVGYLAYIFP LMVAFAAWVF FRNRHEEQDI PTKWPLLILR
     AVGFLLILLA GSALAAIHLG TLDANLPYNG GGIIGVVMAK SLFPIFNTAG TSLILIAFLL
     IGITLFTGLS WFQFLELLGK NAIKFTKFCA IRLGAISWKD LFLSLLPSQD KREAVTVPKI
     KRVEPDLVPD ALDMISTPKI AERPKLEIID HEFKTPRFKG SAILPELSLL DKPSQDHTLS
     YSEEELQQKS REVELRLADF GIQAKVVAVH PGPVVTRFEL QLAAGTKASR VTNLAKDLAR
     SLSVISVRIV EVIPGKSVIG LELPNKNREV VTIYEVLATK QYQNARSSLT LALGKDIGGH
     PVIVDLAKMP HLLVAGTTGS GKSVSLNAML LSLLYKSTPQ QLRLILIDPK MLELSVYEGI
     PHLLTPVVTD MKDAAAALRW CVVEMERRYR LMASLGVRNI LGYNAKVKEA IEAGAPLLDP
     LQAAAEGKPP ELQELPQLVV IADEFADMMV VVGKKVETLI VRLAQKARAA GIHLIFATQR
     PSVDVITGLI KANIPTRVAF QVSSKIDSRT ILDQQGAEQL LGHGDLLYLA PGSGVPVRVH
     GPYVKDEEVH RVAEYLRESS EPNYVEGILD EMGAQDLSGF VEAALGGGSE EGGESDPLYD
     EAVEAVIRSR RVSVSSIQRR FKIGYNRAAR IVEAMEAAGV VSPMENNGAR EVLAPSKE
//