ID A0A1I2END3_9ACTN Unreviewed; 933 AA.
AC A0A1I2END3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=DNA translocase FtsK {ECO:0000313|EMBL:SFE94006.1};
GN ORFNames=SAMN05216251_106289 {ECO:0000313|EMBL:SFE94006.1};
OS Actinacidiphila alni.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=380248 {ECO:0000313|EMBL:SFE94006.1, ECO:0000313|Proteomes:UP000199323};
RN [1] {ECO:0000313|EMBL:SFE94006.1, ECO:0000313|Proteomes:UP000199323}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3510 {ECO:0000313|EMBL:SFE94006.1,
RC ECO:0000313|Proteomes:UP000199323};
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 -!- SIMILARITY: Belongs to the FtsK/SpoIIIE/SftA family.
CC {ECO:0000256|ARBA:ARBA00006474}.
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DR EMBL; FONG01000006; SFE94006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2END3; -.
DR STRING; 380248.SAMN05216251_106289; -.
DR Proteomes; UP000199323; Unassembled WGS sequence.
DR GO; GO:0016020; C: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 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; 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; 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}; DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000199323};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 107..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..162
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..192
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..252
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 581..781
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 283..363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 400..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 598..605
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 933 AA; 98270 MW; EC2F0736ECF00AC2 CRC64;
MFPDRKGGNL GTMASRTSGT AKKAPAKPAA KKTAAKKPAA AKSAAGRPPA KKAAAARPAP
RPAPSPTSGL YRMIRALWLG LAHTVGAVFR GIGNGARGLD PAHRKDGLAL GLLGLTLVVA
AGTWSNLQGP VGDLVEVLVT GAFGRLDLLV PFLLGAIVVR LMRHPEQPEA NGRIVIGLSA
LVIGTLGLVH LACGAPGRDE GATALRDAGG LIGWAAASPL VYTVGSALAV PLLLLFTGFG
FLVVTATPVN AIPQRLRQAG SRLGLYEAPP DPEAVPLEEF FEDDEPAGRR DPEDESPVRR
VPLRFGKSAA EPYDVDRDTD PDERSANRSA AAIADTDAED EPKPRRRPKR RTEKQPGDGE
GPDAVDVAAA AAAALDGAVL HGVQPSPLVA DLTSRIRKPV PAARAEDVPE PEESGGVPDL
TKPSLESTGS PLPPRAEQLQ LSGDITYALP SLDLLERGGP GRTRSAANDA VVASLGQVFK
EFKVDAVVTG FTRGPTVTRY EVELGPAVKV ERITALAKNI AYSVASPDVR IISPIPGKSA
VGIEIPNSDR EMVNLGDVLR SADAAGEDHP MTVALGKDVE GGYVMANLAK MPHVLVAGAT
GSGKSSCINC LITSVMVRAT PDEVRMVLVD PKRVELTAYE GIPHLITPII TNPKRAAEAL
QWVVREMDLR YDDLAAYGFR HIDDFNAAVR SGKAKTPEGS ERELAPYPYL LVIVDELADL
MMVAPRDVED SIVRITQLAR AAGIHLVLAT QRPSVDVVTG LIKANVPSRL AFATSSLADS
RVILDQPGAE KLIGKGDGLF LPMGANKPIR MQGAFVTEDE VAKVVDHCKA QLTPTYRSDV
TVGSGPKKEI DEEIGDDLDL LCQAAELVVS TQFGSTSMLQ RKLRVGFAKA GRLMDLMESR
GIVGPSEGSK ARDVLVKADE LDGVITEIRG GEG
//
