ID A0A0C2BWN0_9BURK Unreviewed; 778 AA.
AC A0A0C2BWN0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KIF82406.1};
GN ORFNames=TSA66_18850 {ECO:0000313|EMBL:KIF82406.1};
OS Noviherbaspirillum autotrophicum.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Noviherbaspirillum.
OX NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF82406.1, ECO:0000313|Proteomes:UP000031572};
RN [1] {ECO:0000313|EMBL:KIF82406.1, ECO:0000313|Proteomes:UP000031572}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSA66 {ECO:0000313|EMBL:KIF82406.1,
RC ECO:0000313|Proteomes:UP000031572};
RA Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL Submitted (DEC-2014) 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:KIF82406.1}.
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DR EMBL; JWJG01000028; KIF82406.1; -; Genomic_DNA.
DR RefSeq; WP_040041080.1; NZ_JWJG01000028.1.
DR AlphaFoldDB; A0A0C2BWN0; -.
DR STRING; 709839.TSA66_18850; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000031572; 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, ECO:0000313|EMBL:KIF82406.1};
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:UP000031572};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 33..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 73..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 420..629
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 759..778
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..444
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 778 AA; 85485 MW; 115B57386A9D495D CRC64;
MTRTAQAYTR NTDPTPENPL PNRLVRLLSE ARWFALTAAT VYLILIFLTY SKADPGWSHA
NVVPRLHNWG GHIGAWLADL MLFIFGFSAW WCCVYMVRLV WAGYRRLSHR FLFQKELEPE
HHHEVWIRSI GFVLMLIGSV AIEYLRMYTL KVQLPRAPGG VLGELVGGAA QNAFGFTGAT
LFLLLLFGVG FSLFFHVSWL AVAERIGGWI EDGANAVRHR YTEREDRKIG QVAAVKREEV
VVQERAKVVE APPIRIEPQV VEVPKSERVQ KEKQVSLFAD LPDTNLPPLS LLDEPPPAQE
TVSVETLEFT SRLIEKKLSD FGVEAKVVAA YPGPVITRYE IEPATGVKGS QIVNLARDLA
RSLSLTSIRV VETIPGKNYM GLELPNPKRQ IVRLTEILGS KVYNDSASSL TVALGKDIAG
NPVVADLAKM PHLLVAGTTG SGKSVGINAT ILSLLYKSDP NNVRMILIDP KMLEMSVYEG
IPHLLAPVVT DMRQAGHALN WAVAEMERRY KLMSKLGVRN LAGYNQKIAE AEKKEEKIPN
PFSLTPDAPE PLDKLPTIVI IIDELADLMM VVGKKVEELI ARIAQKARAA GIHLILATQR
PSVDVITGLI KANIPTRIAF QVSSKIDSRT ILDQMGAETL LGMGDMLYMP PGTGLPVRVH
GAFVSDDEVH RVVQHLKAQG EPNYVEGILE GGVAEEGGDA ALGGEGGGNG EADPMYDQAV
AVVLKNRRAS ISLVQRHLRI GYNRAARLLE QMEQSGLVSS MQSNGNREIL VPAGNNSE
//
