ID A0A1H9LQI0_9PSEU Unreviewed; 794 AA.
AC A0A1H9LQI0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SER13752.1};
GN ORFNames=SAMN04488000_106226 {ECO:0000313|EMBL:SER13752.1};
OS Lentzea albida.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Lentzea.
OX NCBI_TaxID=65499 {ECO:0000313|EMBL:SER13752.1, ECO:0000313|Proteomes:UP000199503};
RN [1] {ECO:0000313|EMBL:SER13752.1, ECO:0000313|Proteomes:UP000199503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44437 {ECO:0000313|EMBL:SER13752.1,
RC ECO:0000313|Proteomes:UP000199503};
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. 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; FOFV01000006; SER13752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9LQI0; -.
DR STRING; 65499.SAMN04488000_106226; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000199503; 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};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 139..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 437..637
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..290
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 271..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 454..461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 794 AA; 85322 MW; 9BF75D30F9B90F6C CRC64;
MAGRTGTSRK TTSRGKAPAK PRARSTASRK PAARKSGGAI SAVWGALGRG VGSVVRTVSR
TKDLDPEHRR DGLGLLLIAL AFITGAGVWW QAGGPVGQWV DVAVRSSVGF PAVVVPVVLL
GIGVTLMRTD PKPDARPRLI IGSFLMIIGV LGMFHLIGGL PMDPLERRDA GGALGYLAGG
FLAQGLTPWV AGPLLFLIFA YGLLVVTHTP IRQAPERIRS LLHPGKPAEP SPFDEEEPVE
EPKPVRLRRP SRRRQAVEPV AEDEPQAELP LEEPVEPPPP SPKPSKKAAA APALVVRAVE
GEYQLPPPDV LKDGDAPKTR SRANDQMIEA ITGVLDQFSI DAQVTGFTRG PTVTRYEVEL
GPGVKVEKIT ALTKNIAYAV ATDNVRLLAP IPGKSAVGIE VPNSDREMVR LGDVLRAPST
VKDTHPMVIG LGKDIEGHMV TANLTKMPHL LVAGSTGSGK SSFVNSMLVS LLARATPDEV
RMILIDPKMV ELTPYEGIPH LITPIITQPK KAAAALAWLV EEMEQRYQDM QVNRVRHVDD
FNRKVKSGEI TAPPGSERVY RPYPYIMAIV DELADLMMTA PRDVEDAIVR ITQKARAAGI
HLVLATQRPS VDVVTGLIKT NVPSRLAFAT SSLTDSRVIL DQPGAEKLIG MGDALYLPMG
AGKPVRIQGA FVGDEEISSI VEFTKNQAQP EYTDGVTAQK AGEKKEIDAD IGDDLELLVQ
ATELIVTSQF GSTSMLQRKL RVGFAKAGRL MDLLETRGVV GPSEGSKARE VLIKPDELEN
VVYLMRGGGP ADDE
//
