ID A0A0G9GYV1_9GAMM Unreviewed; 854 AA.
AC A0A0G9GYV1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=Y882_15770 {ECO:0000313|EMBL:KLD62508.1};
OS Dyella japonica DSM 16301.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1440762 {ECO:0000313|EMBL:KLD62508.1, ECO:0000313|Proteomes:UP000035481};
RN [1] {ECO:0000313|EMBL:KLD62508.1, ECO:0000313|Proteomes:UP000035481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16301 {ECO:0000313|EMBL:KLD62508.1,
RC ECO:0000313|Proteomes:UP000035481};
RX PubMed=25481407; DOI=10.1007/s10482-014-0344-8;
RA Naushad S., Adeolu M., Wong S., Sohail M., Schellhorn H.E., Gupta R.S.;
RT "A phylogenomic and molecular marker based taxonomic framework for the
RT order Xanthomonadales: proposal to transfer the families Algiphilaceae and
RT Solimonadaceae to the order Nevskiales ord. nov. and to create a new family
RT within the order Xanthomonadales, the family Rhodanobacteraceae fam. nov.,
RT containing the genus Rhodanobacter and its closest relatives.";
RL Antonie Van Leeuwenhoek 107:467-485(2015).
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:KLD62508.1}.
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DR EMBL; JPLA01000044; KLD62508.1; -; Genomic_DNA.
DR RefSeq; WP_046972859.1; NZ_JPLA01000044.1.
DR AlphaFoldDB; A0A0G9GYV1; -.
DR STRING; 1440762.Y882_15770; -.
DR PATRIC; fig|1440762.4.peg.2878; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000035481; 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:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007059; P:chromosome segregation; 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, ECO:0000313|EMBL:KLD62508.1};
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 6..23
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 43..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..108
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 500..709
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 148..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..199
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 517..524
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 854 AA; 90461 MW; 760F2752D2A78A3E CRC64;
MLSFFFGAFG LSTLWLVPLF RRVGRSLLKR RHGSGGGKGS IRYGLGALLV LLASATLEGL
LIDQYTDDAN AGGAVCRALS HGIGGLLGGW LATLIMLALL AAALPWYLGM GWPAMFKRLS
AGVDVIASLL QRALDAIAAR RGRPVTRRRA TGAVRRVERA PAKSRRPMPA AQRAAVDPVA
AAKSTAPSAS PTSPAVSSSR IAPVRYAAQQ EKVIREPWLT PKHGRVAASS PGVPLGRTAP
ANATSAVKST AAPMAASVAT AQAPRPIEPI MPAPLPIQIE PVVDDVPLVA STAVDPVPLD
DVATATPAED TSFDVDLAAV ALPLQAVPIA SGRRIAANDD EPANAPAEIA ALPLAPPART
RSTAILPPLS LLAAPRLEQT SIDDVQLAET GELIEQRLRE FKVPVTVVGA SAGPVITRFE
VEPAVGVRGN QIVALMKDLA RGLGRTSIRV VETIPGKTCM GLELPNEQRQ MIALSEILDS
PAYRDADSLL TLAMGKGITG EPVVADLAKA PHMLVAGTTG SGKSVAVNAM ILSMLYKATP
DDVRMIMIDP KMLELSVYEG IPHLLAPVVT DMKLAANALA WCVAEMENRY RVMSDLRVRN
LAGFNQKVRE ARAAGRPLMN PFPAHPEVPE LLDTLPMIVV VIDELADLMM VAGKKIEELI
ARLAQKARAA GIHLILATQR PSVDVITGLI KANIPTRVAF QVSSKIDSRT ILDQMGAESL
LGQGDMLFLP PGTGYPQRIH GAFVADEEVH RIVAHLKLYG EPDYKDEILA GPPSEGSGDL
LTEEGGDAEL DPLYDEAAAF VLRSRRASIS FVQRQFRIGY NRAARLVEAM EAAGLVSSMG
INGQREVIAP GPSD
//
