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Database: UniProt
Entry: A0A1L9NWZ8_9RHOB
LinkDB: A0A1L9NWZ8_9RHOB
Original site: A0A1L9NWZ8_9RHOB 
ID   A0A1L9NWZ8_9RHOB        Unreviewed;      1043 AA.
AC   A0A1L9NWZ8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN   Name=ftsK {ECO:0000313|EMBL:OJI93810.1};
GN   ORFNames=PFRI_19570 {ECO:0000313|EMBL:OJI93810.1};
OS   Planktotalea frisia.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Planktotalea.
OX   NCBI_TaxID=696762 {ECO:0000313|EMBL:OJI93810.1, ECO:0000313|Proteomes:UP000184514};
RN   [1] {ECO:0000313|EMBL:OJI93810.1, ECO:0000313|Proteomes:UP000184514}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH6-1 {ECO:0000313|EMBL:OJI93810.1,
RC   ECO:0000313|Proteomes:UP000184514};
RA   Poehlein A., Bakenhus I., Voget S., Brinkhoff T., Simon M.;
RT   "Genome sequence of Planktotalea frisia SH6-1.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OJI93810.1}.
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DR   EMBL; MLCB01000130; OJI93810.1; -; Genomic_DNA.
DR   RefSeq; WP_072630523.1; NZ_QKZM01000021.1.
DR   AlphaFoldDB; A0A1L9NWZ8; -.
DR   STRING; 696762.PFRI_19570; -.
DR   Proteomes; UP000184514; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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; SM00382; AAA; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184514};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        27..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        68..95
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        107..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        166..188
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        194..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          678..897
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         695..702
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1043 AA;  112506 MW;  F3AA10D07B376358 CRC64;
     MAYQARGRDP LLDSNMQAMI EKRGKEMIGA ALIIFGILAA MVVGSYTPTD PSWLSATDAP
     VQNWLGQLGA SIAAPLFMIV GKAAWVIPVV SLGWGVRFVL HFGAERALGR IIFLPIAVVV
     CAVYMSSLVP GAGWTHTFGL GGLFGDTVLG AFLTFLPFSA TVGLKLIAFF LAIATVAMLA
     FVLGATRYEL KESARFLAIG VVVTYMMAMR LIGKGAKGAV GAASTLQARQ TEKRDALRAE
     DEARAARRLA DEPRMSHIAS EPVIEPVYEE PEPAPEKEKL GLLARMPSLI KRADPMPEPE
     LVEQQALENY AEMPTDDRIK SKISNVIKSR ARNHMVTQPP VSSHPAKSRS RGPIPLVVDT
     TLPNMRVEPP LSASLIAQPP LAEMAEPSAL AFTSARMEAV AEPAEPVEAP IMQEPVAQAP
     AFLSASYQTQ PPLEQPVPQE PMAYVAPAAS MPEPTLAPVT SFDAMPTEYL PTPELADVPS
     FESAPLVTEE EIATFAPLPD PVPAPAPKSV VQHAQRKPMQ PSTRAKAEAQ PTLKFADSKE
     AFELPPLNLL ESPSTVQRHH LSDEALEANA RMLEAVLDDY GVKGEIVSVR PGPVVTMYEL
     EPAPGLKASR VIGLSDDIAR SMSALSARVS TVPGRSVIGI ELPNENREKV VLREILSSRD
     FGDGQQKLPL ALGKDIGGDP IVANLAKMPH LLIAGTTGSG KSVAINTMIL SLLYKLTPEE
     CRLIMIDPKM LELSVYDGIP HLLSPVVTDP KKAVVALKWT VGEMEERYRK MSKMGVRNID
     GYNSRVADAL GKNEMFSRTV QTGFDDETGE PIFETEETQP EKMPYIVVVV DEMADLMMVA
     GKEIEACIQR LAQMARASGI HLIMATQRPS VDVITGTIKA NFPTRISFQV TSKIDSRTIL
     GEMGAEQLLG MGDMLYMAGG AKITRCHGPF VSDEEVEEIV NHLKGYGPPN YMSGVVEGPS
     EDAASSIDTV LGLGGNTDGE DALYDTAVAI VVKDRKCSTS YIQRKLAIGY NKAARLVEQM
     EDEGLVSPAN HVGKREILVP EAQ
//
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