ID A0A1H3LIR9_9PROT Unreviewed; 768 AA.
AC A0A1H3LIR9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SDY63858.1};
GN ORFNames=SAMN05421881_104917 {ECO:0000313|EMBL:SDY63858.1};
OS Nitrosomonas halophila.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=44576 {ECO:0000313|EMBL:SDY63858.1, ECO:0000313|Proteomes:UP000198640};
RN [1] {ECO:0000313|EMBL:SDY63858.1, ECO:0000313|Proteomes:UP000198640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm1 {ECO:0000313|EMBL:SDY63858.1,
RC ECO:0000313|Proteomes:UP000198640};
RA de Groot N.N.;
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}.
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DR EMBL; FNOY01000049; SDY63858.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3LIR9; -.
DR STRING; 44576.SAMN05421881_104917; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000198640; 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:UP000198640};
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..47
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 77..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 162..184
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 410..619
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 683..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 427..434
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 768 AA; 83671 MW; F62E75B848659A0A CRC64;
MSFANKSMAK KSASNPLPPR ISRLLREAVS LILGGIALYL ALILISFDHT DPGWSRSAAS
QLVSNAGGSA GAWLSDLLLY LFGVSAWWWV VFFLAAVWWS YRRIDIASVF DPRALLVSFT
GFITLLIASS GIESLRFHTL KAPLPLAPGG ILGEVLSKQL SLVLGFTGTT LGLVILFAIG
LSLFSGLSWV RLSEKIGTAI EAACLALKDL WVAWQDRRAG MASTQRREVH VEEIKKQLLP
QTPLHIEMPE TTIQKAPRVN KEKHTPLFSD VADSPLPPLY LLDEPDKNVE VLSSDTLEFT
SRLIERKLLE FGVEVKVVAA YPGPVITRYE IEPAVGVKGN QIVNLVRDLA RALTVASIRV
VETIPGKTTM GLEIPNPKRQ VVRLHEILAS KVYADHASPL TIALGKDISG RPIVSDLAKM
PHALVAGTTG SGKSVAINAV ILSLVYKAPP ETVRLILIDP KMLELSVYEG IPHLLTPVVT
DMRDAASALN WCVAEMERRY KLMSALGVRN LAGYNQKVRE AIKKEEPLTN PLSTTPDSPE
LLEEIPLIVV VIDELADLMM IVGKKVEKLI ARLAQKARAA GIHLLLATQR PSVDVITGLI
KANIPTRIAF QVSSKIDSRT ILDQMGAEAL LGQGDMLYLP PGSGYPQRVH GAFVADHEVH
KVVEYLKEHG EARYVEEILQ AGDEDGSAGD NGTGENGKAG GGESDPLYDE AVSIVVKSRR
ASISLVQRQL RIGYNRAARL IEEMERAGLV SSMQSNGNRE VLAPKRDE
//
