ID   FTSK_VIBVU              Reviewed;         985 AA.
AC   Q8D8M2;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=DNA translocase FtsK;
GN   Name=ftsK; OrderedLocusNames=VV1_2950;
OS   Vibrio vulnificus (strain CMCP6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=216895;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMCP6;
RA   Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT   "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   SEQUENCE REVISION TO C-TERMINUS.
RC   STRAIN=CMCP6;
RX   PubMed=21245845; DOI=10.1038/msb.2010.115;
RA   Kim H.U., Kim S.Y., Jeong H., Kim T.Y., Kim J.J., Choy H.E., Yi K.Y.,
RA   Rhee J.H., Lee S.Y.;
RT   "Integrative genome-scale metabolic analysis of Vibrio vulnificus for drug
RT   targeting and discovery.";
RL   Mol. Syst. Biol. 7:460-460(2011).
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; AE016795; AAO11281.2; -; Genomic_DNA.
DR   RefSeq; WP_011080766.1; NC_004459.3.
DR   AlphaFoldDB; Q8D8M2; -.
DR   SMR; Q8D8M2; -.
DR   EnsemblBacteria; AAO11281; AAO11281; VV1_2950.
DR   KEGG; vvu:VV1_2950; -.
DR   HOGENOM; CLU_001981_0_2_6; -.
DR   Proteomes; UP000002275; Chromosome 1.
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   Transmembrane; Transmembrane helix.
FT   CHAIN           1..985
FT                   /note="DNA translocase FtsK"
FT                   /id="PRO_0000098318"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        117..137
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        145..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        195..985
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          626..839
FT                   /note="FtsK"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
FT   BINDING         646..651
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   985 AA;  108746 MW;  1D60C80C975BB22A CRC64;
     MFKENAKKVQ TIIKTSEEAQ SSRLNGFQRL KECCLILGVL TSAFLSIALL TFSPADPSWS
     QTSWGGDISN AGGQFGAWVA DTLFFTFGLL AYLLPVLLVI VTWVFFRTRD EDEHIDLMLW
     GTRLLGLAIL ILTSCGLADI NFDDIWYFSS GGVLGDVLNS LALPTLNLLG TTLVLLFAWG
     AGFTLLTGIS WLSIVEWIGS LFLDVCQWAL NRLRGEKTEV IAPELQPIAL SDDEPKAQPQ
     IEAQQDEIVE EERIPDPLPV EPVVQMRREY PIHMPQTVSY QTVSDELDEL EDNSFERAKK
     LNATIEELEQ EALSVNDLPD DTMSTERARY NVADIAQVSA EHSQTTQVEH AQDFSVDVEE
     FDHVISLSEL DKISEEIDEP VMVGFAEEAP LHHNEAQRSA MASSAEPMFS HLGVEQTTQH
     TTQEEIVDLP VADSVGDVNP EMEDYVEEDE DQDQDVVAFQ NMVSKAQQNM AATQNPFLMK
     QDTSLPVPKE PLPTLELLYH PEKRENFIDK EALEQVARLV ESKLADYKIT AEVVGIFPGP
     VITRFELDLA PGVKVSRISS LSMDLARSLS AMAVRVVEVI PGKPYVGLEL PNMSRQTVYL
     SDVIDSPQFQ NATSPTTVVL GQDIAGEALV ADLAKMPHVL VAGTTGSGKS VGVNVMILSM
     LYKASPEDVR FIMIDPKMLE LSVYEGIPHL LAEVVTDMKD ASNALRWCVG EMERRYKLMS
     VMGVRNIKGF NEKLKMAADA GHPIHDPFWQ EGDSMDTEPP LLEKLPYIVV VVDEFADLMM
     VVGKKVEELI ARLAQKARAA GIHLILATQR PSVDVITGLI KANIPTRVAF TVSTKTDSRT
     ILDQGGAESL LGMGDMLYLP PGSSHTIRVH GAFASDDDVH AVVNNWKARG KPNYIDEIIS
     GEQGPESLLP GEQMESDEDL DPLFDQVVEH VVQSRRGSVS GVQRRFKIGY NRAARIVEQL
     EAQGIVSAPG HNGNREVLAP APPRE