ID A0A1H6ZEK6_9MICO Unreviewed; 898 AA.
AC A0A1H6ZEK6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SEJ47970.1};
GN ORFNames=SAMN05421637_1947 {ECO:0000313|EMBL:SEJ47970.1};
OS Demequina mangrovi.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Demequinaceae;
OC Demequina.
OX NCBI_TaxID=1043493 {ECO:0000313|EMBL:SEJ47970.1, ECO:0000313|Proteomes:UP000183315};
RN [1] {ECO:0000313|Proteomes:UP000183315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24868 {ECO:0000313|Proteomes:UP000183315};
RA Varghese 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. Required for activation of the Xer recombinase, allowing
CC activation of chromosome unlinking by recombination.
CC {ECO:0000256|ARBA:ARBA00024986}.
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; FNZI01000004; SEJ47970.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ZEK6; -.
DR STRING; 1043493.SAMN05421637_1947; -.
DR eggNOG; COG1674; Bacteria.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000183315; 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};
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:UP000183315};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 74..92
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..129
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 141..159
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 179..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 527..727
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 876..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 544..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 898 AA; 95780 MW; 36AB7516743AB7AD CRC64;
MAQTRQSRPA PRTQQAKRSS SSSSRSTAQA KRRPPALLRG IAAIGRGTSN ALGSGVRSIG
HGARDVPPAV RRDGIAITLV ILAILIAARE WFQLPSWAGT GIHWVVAGLF GLLAYGVPVV
LGIIAVRLMR APQEEGTNHR ITLGALLLAI MVDGIIHIAK DQPGPTDGAQ GLQDAGGVLG
FLIGTPLAML VTVPLAIVVL VLVALLAVLI IFGVSMREAA AWVGEVASKV RADHGDGGES
TDSDELDLPE HRTLERPGDT KVIKPAKGRA KRMLDRAIHG EQPAAEEDSL DAYEADEAFA
QAASVERTEF DDIIDPDGAH APATEVISPY AVEEDAPWGD PEPAPWDPEP EPQQAPQDVA
TQLIEVQEDV HAPEATHLVP EGEQGVLENS LPYVLPSLEI LAKGAPHKER SAANDRVVAS
LTNVLEQFGV DAEVTGFTRG PTVTRYEVEL GAGVKVEKIT QLSKNIAYAV ASADVRILSP
IPGKSAIGIE IPNVDRETVA LGDVLRSQVA ARNDHPMAIG IGKDVEGGYV MANLAKMPHL
LVAGATGAGK SSFVNSMITS ILMRATPNEV RMVLVDPKRV ELTIYEGIPH LITPIITDPK
KAAQALEWVV KEMDMRYDDL ALFGYKHIDD FNKGVRAGKV KPLPGSERKI KTYPYLLVIV
DELADLMMVA PRDVEESIQR ITQLARAAGI HLVLATQRPS VDIITGTIKA NVPSRLAFAT
SSLADSRVVL DTPGAEKLIG QGDALFLPMG ESKPMRAQGS WVSESEIHAA VEHAKRQADP
EYREDVVQAT TTAGAVAEDI GDDLEDLLQA AELVITTQLG STSMLQRKLK MGFAKAGRLM
DLLETREIVG PSQGSKARDV LVTPDDLAST LAVLRGDGGA TVGSTPTPEA EDEEWVES
//
