ID M1PQA5_DESSD Unreviewed; 727 AA.
AC M1PQA5;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=DNA segregation ATPase, FtsK/SpoIIIE family {ECO:0000313|EMBL:AGF78571.1};
GN OrderedLocusNames=UWK_02022 {ECO:0000313|EMBL:AGF78571.1};
OS Desulfocapsa sulfexigens (strain DSM 10523 / SB164P1).
OC Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC Desulfocapsaceae; Desulfocapsa.
OX NCBI_TaxID=1167006 {ECO:0000313|EMBL:AGF78571.1, ECO:0000313|Proteomes:UP000011721};
RN [1] {ECO:0000313|Proteomes:UP000011721}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10523 / SB164P1 {ECO:0000313|Proteomes:UP000011721};
RX PubMed=23961312; DOI=10.4056/sigs.3777412;
RA Finster K.W., Kjeldsen K.U., Kube M., Reinhardt R., Mussmann M., Amann R.,
RA Schreiber L.;
RT "Complete genome sequence of Desulfocapsa sulfexigens, a marine
RT deltaproteobacterium specialized in disproportionating inorganic sulfur
RT compounds.";
RL Stand. Genomic Sci. 8:58-68(2013).
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; CP003985; AGF78571.1; -; Genomic_DNA.
DR RefSeq; WP_015404262.1; NC_020304.1.
DR AlphaFoldDB; M1PQA5; -.
DR STRING; 1167006.UWK_02022; -.
DR KEGG; dsf:UWK_02022; -.
DR PATRIC; fig|1167006.5.peg.2211; -.
DR eggNOG; COG1674; Bacteria.
DR HOGENOM; CLU_001981_9_6_7; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000011721; 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 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:UP000011721};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 50..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 130..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 395..581
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 638..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..658
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 412..419
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 727 AA; 78563 MW; 53E7C4BFCD9EFF7F CRC64;
MTQVSKKTRP SLKQEATAVL GVFLSLFLFL SLASPYFAGD GNWGGEIGML IAQILTGVTG
WGAYLLAALL LILSFLFFSP RVAFERLPQI TAGLTGSVLS ACALFSAFSL KGWASIDAGG
VIGKTIFTVM QSLVGGPGTV LFLLLIFLMS FMLSTQFSPY QLTLFLWRVT KKAGCGLRNI
LVFGNERRVM RKEAKRSAKT VTAVENGPRV RIPSGRVGRE TPDAVGPSLG MPVVKEIAKT
SEVSDDDDFA ARLVARGDWK LPPISLLEKN SSQGGVVDKE VYYQVSKKLE QKLKNFGVSG
KVVGISPGPV VTTYEYSPAA GVKINKIAGL ADDLALGLKA QSVRVVGSVP GKAALGIEIP
NPNRSVVYIR DLLASEEYRK VEDKLAIVLG LDVVGAPSIV NLAKMPHLLI AGSTGSGKSV
AINTIIASIL YNATPEEVRL LMVDPKRIEL SGYEGIPHLL HPVVVEPKLA SRALMWAVRE
MERRYKLLEV ARVKSFDSYN ESAEEKLPYI VIIVDELADL MMVASKDVES SIARLAQMAR
AAGMHLILAT QRPSVDVLTG LIKANFPTRI SFKVSSKIDS RTILDTSGAE HLLGAGDMLY
LANGSSGLQR VHGAYISEAE TEAIITFLKE QGNASYDESV TSAVEDEGND GEAAGDEEYD
ERYDEAVNLV CESGQASISM VQRRLRVGYN RAARMIEMME KEGVVGPADG AKPREVFARK
DYTSELI
//
