ID   FTSK_MYCTO              Reviewed;         831 AA.
AC   P9WNA2; L0TDF9; O33290;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 37.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=MT2819;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(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. 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 membrane {ECO:0000250}; Multi-pass membrane
CC       protein {ECO:0000250}. Note=Located at the septum. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47139.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47139.1; ALT_INIT; Genomic_DNA.
DR   PIR; C70879; C70879.
DR   AlphaFoldDB; P9WNA2; -.
DR   SMR; P9WNA2; -.
DR   EnsemblBacteria; AAK47139; AAK47139; MT2819.
DR   KEGG; mtc:MT2819; -.
DR   HOGENOM; CLU_001981_2_1_11; -.
DR   Proteomes; UP000001020; 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 membrane;
KW   Chromosome partition; DNA-binding; Membrane; Nucleotide-binding;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..831
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000427162"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        164..184
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        214..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        235..831
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          476..676
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          1..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          296..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..26
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..48
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         496..501
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   831 AA;  88887 MW;  DDCFA08FE57A6135 CRC64;
     MSSKTVARSG TRTSRSKATS RGASRSARSA VPRKRSRPVK GVGRPSRRHH RSLLVSTGLA
     CGRAMRAVWM MAAKGTGGAA RSIGRARDIE PGHRRDGIAL VLLGLAVVVA ASSWFDAARP
     LGAWVDALLR TFIGSAVVML PLVAAAVAVV LMRTSPNPDS RPRLILGASL IGLSFLGLCH
     LWAGSPEAPE SRLRAAGFIG FAIGGPLSDG LTAWIAAPLL FIGALFGLLL LAGITIREVP
     DAMRAMFGTR LLPREYADDF EDFADFDGDD ADTVEVARQD FSDGYYDEVP LCSDDGPPAW
     PSAEVPQDDT ATIPEASAGR GSGRRGRRKD TQVLDRIVEG PYTLPSLDLL ISGDPPKKRS
     AANTHMAGAI GEVLTQFKVD AAVTGCTRGP TVTRYEVELG PGVKVEKITA LQRNIAYAVA
     TESVRMLAPI PGKSAVGIEV PNTDREMVRL ADVLTARETR RDHHPLVIGL GKDIEGDFIS
     ANLAKMPHLL VAGSTGSGKS SFVNSMLVSL LTRATPEEVR MILIDPKMVE LTPYEGIPHL
     ITPIITQPKK AAAALAWLVD EMEQRYQDMQ ASRVRHIDDF NDKVRSGAIT APLGSQREYR
     PYPYVVAIVD ELADLMMTAP RDVEDAIVRI TQKARAAGIH LVLATQRPSV DVVTGLIKTN
     VPSRLAFATS SLTDSRVILD QAGAEKLIGM GDGLFLPMGA SKPLRLQGAY VSDEEIHAVV
     TACKEQAEPE YTEGVTTAKP TAERTDVDPD IGDDMDVFLQ AVELVVSSQF GSTSMLQRKL
     RVGFAKAGRL MDLMETRGIV GPSEGSKARE VLVKPDELAG TLAAIRGDGG E