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Database: UniProt
Entry: J2ZWM7_9CAUL
LinkDB: J2ZWM7_9CAUL
Original site: J2ZWM7_9CAUL 
ID   J2ZWM7_9CAUL            Unreviewed;       806 AA.
AC   J2ZWM7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   ORFNames=PMI01_04750 {ECO:0000313|EMBL:EJL23746.1};
OS   Caulobacter sp. AP07.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL23746.1, ECO:0000313|Proteomes:UP000007300};
RN   [1] {ECO:0000313|EMBL:EJL23746.1, ECO:0000313|Proteomes:UP000007300}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP07 {ECO:0000313|EMBL:EJL23746.1,
RC   ECO:0000313|Proteomes:UP000007300};
RX   PubMed=23045501; DOI=10.1128/JB.01243-12;
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA   Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT   "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT   sequences from diverse bacteria isolated from the rhizosphere and
RT   endosphere of Populus deltoides.";
RL   J. Bacteriol. 194:5991-5993(2012).
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.
CC       {ECO:0000256|ARBA:ARBA00024784}.
CC   -!- SUBUNIT: Homohexamer. Forms a ring that surrounds DNA.
CC       {ECO:0000256|ARBA:ARBA00025923}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC       {ECO:0000256|ARBA:ARBA00006474}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJL23746.1}.
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DR   EMBL; AKKF01000255; EJL23746.1; -; Genomic_DNA.
DR   RefSeq; WP_007674836.1; NZ_AKKF01000255.1.
DR   AlphaFoldDB; J2ZWM7; -.
DR   PATRIC; fig|1144304.3.peg.4536; -.
DR   Proteomes; UP000007300; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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   CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR   Gene3D; 3.30.980.40; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 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   PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
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; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS50901; FTSK; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Cell cycle {ECO:0000256|ARBA:ARBA00023306};
KW   Cell division {ECO:0000256|ARBA:ARBA00022618};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        31..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        71..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        146..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        172..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          443..661
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          212..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         460..467
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   806 AA;  86230 MW;  BE3F2FCDEA50A980 CRC64;
     MARAARRSSV ELVWDAVRYG WAQPWSARFR GGVICVVGAG LLLAVATYNA TDPSFNAATG
     LPATNALGGP GAALADIVMQ SLGLSGWVAA LLMLVFGMTR VSQADPAAHR RDLRVRALVG
     GLGLLALAGL LAAPPTPAVW KLARGLGGFW GDGLLNTVAG LLAFARLPGA HLIAALLLGI
     GAAVALGYAI GLRRIDPEAV ADALHGLMQP RERAPAAPAP QPEPAAARPR APRKAAAPVI
     EVAPEAAQVP RRAAKPAKPA PAEDDDAFEP SFEVRPLAIA QPKTPNRVNT REQREQQKAF
     DFTDEGGFQL PELAMLAKPK PRSAEFDEEA LRQNARLLES VLAEFGVRGQ IDQIRPGPVV
     TMYELVPAAG TKTARVVALA DDIARSMSVI SCRVAVAQGR NAIGIEMPNS RKETVYLRDL
     LSSADYDKAT HSLPMALGET IGGETYIADL AKMPHLLIAG TTGSGKSVGV NAMILSILYK
     LPPEKCRFIM IDPKMLELSV YDGIPHLLAP VVTDPKKAVV ALKWTVREME DRYRRMSKIG
     VRNIAGYNEK ANEALDKGEH FERTVQTGFD DAGRPIYETE KIRPEAMPFL VVVIDEVADL
     MMVAGKDIEG AVQRLAQMAR AAGIHLIMAT QRPSVDVITG TIKANFPTRI SFQVTSKIDA
     RTILGEQGAE QLLGQGDMLY MAGGGRITRL HGPFVSDGEV EAVAKFLRDQ GIPNYLEEVT
     AGGDEEQEEA IEGAFAGEGG ANDLYDHAVA VVTRDRKAST SYIQRRLQIG YNRAASLMER
     MEKEGVVGAA NHAGKREILA PPPPPM
//
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