ID A0A0M8Y802_9PSEU Unreviewed; 817 AA.
AC A0A0M8Y802;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KOX20338.1};
GN ORFNames=ADK67_30185 {ECO:0000313|EMBL:KOX20338.1};
OS Saccharothrix sp. NRRL B-16348.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharothrix.
OX NCBI_TaxID=1415542 {ECO:0000313|EMBL:KOX20338.1, ECO:0000313|Proteomes:UP000037722};
RN [1] {ECO:0000313|EMBL:KOX20338.1, ECO:0000313|Proteomes:UP000037722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-16348 {ECO:0000313|EMBL:KOX20338.1,
RC ECO:0000313|Proteomes:UP000037722};
RA Noorani M.;
RL Submitted (JUL-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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOX20338.1}.
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DR EMBL; LGED01000218; KOX20338.1; -; Genomic_DNA.
DR RefSeq; WP_053719920.1; NZ_LGED01000218.1.
DR AlphaFoldDB; A0A0M8Y802; -.
DR STRING; 1415542.ADK67_30185; -.
DR PATRIC; fig|1415542.3.peg.6502; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000037722; 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, ECO:0000313|EMBL:KOX20338.1};
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 85..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 123..140
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 152..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 199..220
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 456..656
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 286..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 473..480
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 817 AA; 86758 MW; FA714DDD9E314152 CRC64;
MAGRTGTSRK GTTRSTGSGS KARASASRSG GSRPASKRAP AKRAPAKKSS GSVGKVWGLL
GRGVGSVVRA VGRTKELDPA HRRDGLALVL IAVAVITAAG VWWQAGGPVG QWVDVAVRSS
VGGPAVIFPV VLLAIGVTLM RTDPNPEARP RLVIGSILVA VGFLGMFHLA GGLPMDPLAR
RDAGGALGYL SGGFLAQGLT SWVAGPLLVL IFAYGVLLLV HLPIREVPAK LGGLLHRKPD
QLDGFGAEEA EAEPEPEEKP AKLRRPSRSR RQAVAVPDEQ PELPLDEEPP PPPAAKPAPK
PKATPETPKP AAIAVRAVEG DYRLPPPTIL KDGDAPKARS KANDLMIEAI SGVLDQFSID
AQVTGFTRGP TVTRYEVELG PGVKVEKITA LTKNIAYAVA TDNVRLLAPI PGKSAVGIEV
PNSDREMVRL GDVLRSPSTV KDNHPMVIGL GKDIEGHFVT ANLTKMPHLL VAGSTGSGKS
SFVNSMLVSL LARATPDEVR MILIDPKMVE LTPYEGIPHL ITPIITQPKK AAAALAWLVE
EMEQRYQDMQ VNRVRHIDDF NRKVKSGEIS APPGSERVYR PYPYIMAIVD ELADLMMTAP
RDVEDAIVRI TQKARAAGIH LVLATQRPSV DVVTGLIKTN VPSRLAFATS SLTDSRVILD
QPGAEKLIGM GDGLYLPMGA SKPVRVQGAY VGDDEISEIV NFTKDQAQPE YTDGVTAAKA
GEKKEIDADI GDDLELLIQA AELIVTSQFG STSMLQRKLR VGFAKAGRLM DLLETRGVVG
PSEGSKAREV LIKPDELDSL VYLIRGGSGP GDDGDDD
//