ID J5PS80_9RHOB Unreviewed; 838 AA.
AC J5PS80;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=DNA translocase FtsK {ECO:0000256|ARBA:ARBA00020887};
GN ORFNames=A33M_1399 {ECO:0000313|EMBL:EJW12837.1};
OS Rhodovulum sp. PH10.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1187851 {ECO:0000313|EMBL:EJW12837.1, ECO:0000313|Proteomes:UP000002930};
RN [1] {ECO:0000313|EMBL:EJW12837.1, ECO:0000313|Proteomes:UP000002930}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PH10 {ECO:0000313|EMBL:EJW12837.1,
RC ECO:0000313|Proteomes:UP000002930};
RX PubMed=23105089; DOI=10.1128/JB.01695-12;
RA Khatri I., Nupur, Korpole S., Subramanian S., Pinnaka A.K.;
RT "Draft Genome Sequence of Rhodovulum sp. Strain PH10, a Phototrophic
RT Alphaproteobacterium Isolated from a Soil Sample of Mangrove of Namkhana,
RT India.";
RL J. Bacteriol. 194:6363-6363(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:EJW12837.1}.
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DR EMBL; AKZI01000019; EJW12837.1; -; Genomic_DNA.
DR RefSeq; WP_008383666.1; NZ_AKZI01000019.1.
DR AlphaFoldDB; J5PS80; -.
DR STRING; 1187851.A33M_1399; -.
DR PATRIC; fig|1187851.3.peg.799; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000002930; 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, ECO:0000313|EMBL:EJW12837.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000002930};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 28..49
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 112..134
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 154..183
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 472..691
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 193..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..335
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 293..310
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 489..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 838 AA; 89201 MW; 370AEF6969151C3E CRC64;
MTALRHTGSI ALLPDDLRAA VARRVRQAGG LVLLGAAALC LAALITWSVK DPSLSHATSA
PVRNLLGVPG AIVSDLSMQL FGLAILALIA PIAVWGWRLA HEHRFGRERW RLGAWVLGLP
LAAGFASCLP RSAAWPLPTG LGGVVGDGMV HGPAWIGIGA SVCLVVYGAA AAAAILFACG
VGFTATATDA PKKPAAKAKP AKPVAAPLAP DDPDEDEEDG DRASVSIGLV VHALLSLKAR
ALRLARAGIV AGVKALRERD KEPDTLARDR REPHFGAMPP AADPVAPDAD AQGDAAYEDE
PYDESDEEVE DAPAPAPRNA RKAAPAGRKP KKPAEYELPS LNLLAAPKAS DRNVVPKDVL
EANETALETV LSDFGVRGEI LDAHPGPVVT LYELEPAPGI KSSRVIGLAD DIARSMSAVS
ARVAVVPGRN VIGIELPNAT REKVLFREML ASEQFHDCNA KLPLCLGKTI GGDAVIVDLA
RMPHLLIAGT TGSGKSVAIN TMILSLLYRL RPDQCRLIMV DPKMLELSVY DGIPHLLTPV
VTDPKKAVVA LKWAVREMES RYKKLAKVGV RNIEGYNARL AEAKAKGERL TRTVHTGYDK
ETGTAIYETE ELDLEPLPFI VVVVDEMADL MMVAGKDIEG AVQRLAQMAR AAGLHVIVAT
QRPSVDVITG TIKANFPTRI SFQVTSKIDS RTILGEQGAE QLLGQGDMLY MAGGGRISRV
HGPFVSDEEV EKIVRHLKTQ GAPQYLEDVT AEEESGDGEA VFDGTAMGQE GDLYQQAVAV
VLRDRKASTS YIQRRLQIGY NKAASLMERM EAEGVVGQAN HAGKREILVG GDAEEEAF
//
