ID   FTSK_SHEON              Reviewed;         911 AA.
AC   Q8EER3;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=SO_2306;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(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; AE014299; AAN55345.1; -; Genomic_DNA.
DR   RefSeq; NP_717901.1; NC_004347.2.
DR   RefSeq; WP_011072306.1; NZ_CP053946.1.
DR   AlphaFoldDB; Q8EER3; -.
DR   SMR; Q8EER3; -.
DR   STRING; 211586.SO_2306; -.
DR   PaxDb; Q8EER3; -.
DR   KEGG; son:SO_2306; -.
DR   PATRIC; fig|211586.12.peg.2221; -.
DR   eggNOG; COG0531; Bacteria.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_7_1_6; -.
DR   OMA; SWLTIVD; -.
DR   OrthoDB; 349533at2; -.
DR   PhylomeDB; Q8EER3; -.
DR   BioCyc; SONE211586:G1GMP-2108-MON; -.
DR   Proteomes; UP000008186; 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..911
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098290"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        104..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        182..911
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          550..763
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          403..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         570..575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   911 AA;  100321 MW;  CD5CD2B9675683EA CRC64;
     MSQGNSVRTL SGLQRLLEGG LIICCVLAAY ILLALTSFSP SDPGWSQSHF QGDIKNWTGA
     VGAWIADILL YFFGVTAYIM PIIVASTGWL LFKRAHDLLE IDYFSVALRI IGFLLLILGF
     SALASMNANN IYEFSAGGVA GDVIGQAMLP YFNKLGTTLL LLCFLGSGFT LLTGISWLTV
     VEKIGFVSIW SFKQLKRLPQ ALKREHETED TRGFMSVVDK FKERRDSQHV LDKAKARQPA
     ETPSRVLHTR AIPEESHEEF ITEASSGKGK LSSLVKILSF NSNKAKDEPK SQQRVEPQLD
     QASAVAEYGH FEAPPWVAKS HDAELDDVDT GLNAEFFEDD DGDEPVFHRE TMIDEDDDTL
     SFNDDDVIDF DTKVSAGAVT QAQRQKQTPK AKIVDGIVVL PGQEDKPVPT KPMDPLPSVS
     LLDVPDRKKN PISPEELEQV ARLVEAKLAD FNIVATVVGV YPGPVITRFE LELAPGIKAS
     KISNLANDLA RSLLAERVRV VEVIPGKSYV GLELPNKFRE TVYMRDVLDC EAFSQSKSNL
     TMVLGQDISG EPVVVDLGKM PHLLVAGTTG SGKSVGVNVM ITSLLYKSGP EDVRFIMIDP
     KMLELSVYEG IPHLLCEVVT DMKEAANALR WCVGEMERRY KLMSMMGVRN IKGYNAKIAE
     AKVNGEVIYD PMWKSSDSME PEAPALDKLP SIVVVVDEFA DMMMIVGKKV EELIARIAQK
     ARAAGIHLIL ATQRPSVDVI TGLIKANIPT RMAFQVSSRI DSRTILDQQG AETLLGMGDM
     LYLPPGTAVP NRVHGAFIDD HEVHRVVADW CARGKPQYID EILNGVSEGE QVLLPGETAE
     SDEEYDPLYD EAVAFVTETR RGSISSVQRK FKIGYNRAAR IIEQMEMQGV VSAQGHNGNR
     EVLAPPAPKH Y