FTSK_COXBU
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 03-AUG-2022, entry version 129.
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; Proteobacteria; 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 PRIDE; P39920; -.
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 OMA; SWLTIVD; -.
DR Proteomes; UP000002671; 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 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
