ID A0A0G3V1W9_9ACTN Unreviewed; 869 AA.
AC A0A0G3V1W9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=FtsK/SpoIIIE family protein,Ftsk gamma domain-containing protein {ECO:0000313|EMBL:AKL73119.1};
GN ORFNames=IMCC26256_11826 {ECO:0000313|EMBL:AKL73119.1};
OS Actinobacteria bacterium IMCC26256.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1650658 {ECO:0000313|EMBL:AKL73119.1, ECO:0000313|Proteomes:UP000035517};
RN [1] {ECO:0000313|EMBL:AKL73119.1, ECO:0000313|Proteomes:UP000035517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMCC26256 {ECO:0000313|EMBL:AKL73119.1,
RC ECO:0000313|Proteomes:UP000035517};
RA Kim S.;
RT "Genome sequencing of freshwater Actinobacteria.";
RL Submitted (MAY-2015) 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 -!- 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; CP011489; AKL73119.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G3V1W9; -.
DR STRING; 1650658.IMCC26256_11826; -.
DR KEGG; abai:IMCC26256_11826; -.
DR PATRIC; fig|1650658.3.peg.820; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000035517; Chromosome.
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 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:UP000035517};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 95..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..201
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 517..721
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 29..77
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 778..797
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..63
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 534..541
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 869 AA; 91748 MW; CAA8E7E8883013D9 CRC64;
MWPFGKIVAK GSIVAGVVTV TLNDVAATKT SRARRRTSAR KSNRRVTRRP TTKSTRRGTR
ARSTRSTRST TYTRSPHSRV RVAWTEQLGG HAADAVAIAL VSVGVLTALA LLTDLAGPFG
AACQSAITLL AGRGAFLVPT LCVAVAADLL WHRGPDATSG NKKKTATSKS ASSKSAEEGS
VHLLRIGVGL SLLVGGLLGL LSLGNPVLDT TATALRDSGG IIGALVAVPL SSLLGTVGSA
VVLVAVAATG ALVATGTSLA RVGAALGVAW RSVSGFVSRF LELDGSSDAD ADESDDLNLD
DELESAEAEE KPVRKRRVTV ETVAAPDADS EVKVDAPEPV VAVVPQVVTQ DALPEGSSEL
GEDENEEAED LRLDVSVPAH TNWELPPVNL LRLSQHKELD TRGIEASGAV LEQTLRDFGV
DAQLVGMTVG PTVTRYELEL AAGVKVNKVT GLSHDIAYAM ASADVRILAP IPGRSAIGVE
VPNKQRQLIT LGDILTSDEA AKATHPLEVG LGRDIAGTSV MLNLATMPHL LIAGATGSGK
SSCINSIITS LLLRSTPDQV RLILVDPKRV ELGQYNGLPH LLTEVVANPK RAANALEWCV
REMEMRYELL AEIGARDITG YNAMFDRGDL PTAENPDPLG GRNYDRLPFI VIVIDELNDL
MMVAARDVEN SICRIAQMAR AVGIHLIIAT QRPSVDVITG VIKANVPSRL AFSVTSIADS
RVILDQAGAE KLIGQGDMLA APASGRPARV QGSWVDEDCV RKVVAFWKRQ VTEVQYVDGV
QGSENGSSGG SGDAEDGDDE LLMQAMELVV RSGLGSTSML QRKLRVGFAR AGRLMDLLEN
KGVVGPSEGS KARSVQMTVE EFEEMQARA
//
