ID   FTSK_CORGL              Reviewed;         921 AA.
AC   Q8NP53;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=Cgl1968, cg2158;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC   10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(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. 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=CAF20309.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; BA000036; BAB99361.1; -; Genomic_DNA.
DR   EMBL; BX927153; CAF20309.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_601174.1; NC_003450.3.
DR   AlphaFoldDB; Q8NP53; -.
DR   SMR; Q8NP53; -.
DR   STRING; 196627.cg2158; -.
DR   PRIDE; Q8NP53; -.
DR   KEGG; cgb:cg2158; -.
DR   KEGG; cgl:Cgl1968; -.
DR   PATRIC; fig|196627.13.peg.1905; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_001981_2_1_11; -.
DR   OMA; KPTRMQG; -.
DR   Proteomes; UP000000582; 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   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..921
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098255"
FT   TRANSMEM        69..89
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        105..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        182..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..921
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          533..733
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   REGION          28..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          246..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..290
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        297..313
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         553..558
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   921 AA;  99370 MW;  9A4D0CB669D2CFDB CRC64;
     MTRSIGELGR RRNEDVLDDF DDFEEEIATK PATRKSRSKA VEPEPEFDED FDEQSGNRTS
     AYVEEHADGI ALSLVGIAIV LGAAVWLGIG GPIGTFIADI VHLAIGAGAW ILPVGLIGWA
     VALMLRYTPE RQAQGRVMLG IGVIIVCMLA LIHLFAGNPA EWEGRKTAGG AIGAWIGTPL
     ELGFSVFLAV PILLLLLFWG ALKTTGISIR EFIEFAGGFF GFAGFNRDED EFDEEDDDLY
     GHVERELESR ASGRAPSRTP SRALPKAAPR RTPPLTPPPA PVPAPAPTPA RRPAASLDKY
     PVDDAKAEAP AEPQVKQREA STSILKKPSV TETDEFPAVT EEDLAPAPAS DAVAASRESM
     RQAIIARSGK DPVVEKKPAA PAPVAPTPAD IVSDGDSTYV LPSADLLIPG EPAKLHSETN
     DRMIEAITDV FSEFNVDATV TGFSRGPTVT RYEIELGPGV KVSKITNLQS NIAYAVATEN
     VRLLTPIPGK SAVGIEVPNS DREMVRLGDV LNARATVENK DSMLIGLGKD IEGDFVSYSV
     QKMPHLLVAG STGSGKSAFV NSLLVSLLTR AKPEEVRLIL VDPKMVELTP YEGIPHLITP
     IITQPKKAAA ALQWLVEEME QRYMDMKQTR VRHIKDFNRK IKSGEIETPP GSKREYRAYP
     YIVCVVDELA DLMMTAPKEI EESIVRITQK ARAAGIHLVL ATQRPSVDVV TGLIKTNVPS
     RLAFATSSLT DSRVILDQGG AEKLIGMGDA LFIPQGAGKP QRIQGAFVTD EEIQAVVDMA
     KAQRQPEYTD GVTEDKASEA KKIDADIGND LEDLLEAVEL VVTSQMGSTS MLQRKLRIGF
     AKAGRLMDLM ETRGVVGPSE GSKAREVLVK PEELETILWM LKGADPADAP KEETWDDEVA
     AEAEEAANTT VVQADPSKGV C