ID A0A101NJ60_9ACTN Unreviewed; 1335 AA.
AC A0A101NJ60;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:KUM93947.1};
GN ORFNames=AQI88_24740 {ECO:0000313|EMBL:KUM93947.1};
OS Streptomyces cellostaticus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM93947.1, ECO:0000313|Proteomes:UP000054241};
RN [1] {ECO:0000313|EMBL:KUM93947.1, ECO:0000313|Proteomes:UP000054241}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM93947.1,
RC ECO:0000313|Proteomes:UP000054241};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT for the species Streptomyces cellostaticus.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUM93947.1}.
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DR EMBL; LMWL01000043; KUM93947.1; -; Genomic_DNA.
DR RefSeq; WP_067003163.1; NZ_KQ948027.1.
DR STRING; 67285.AQI88_24740; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000054241; 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:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR023836; EccCa-like_Actinobacteria.
DR InterPro; IPR023837; EccCb-like_Actinobacteria.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR NCBIfam; TIGR03924; T7SS_EccC_a; 1.
DR NCBIfam; TIGR03925; T7SS_EccC_b; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR PROSITE; PS50901; FTSK; 3.
DR PROSITE; PS50206; RHODANESE_3; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000313|EMBL:KUM93947.1};
KW Cell division {ECO:0000313|EMBL:KUM93947.1};
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000054241};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 35..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 468..669
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 824..1015
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 931..966
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 1110..1293
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 97..124
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 491..498
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 842..849
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1128..1135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1335 AA; 142881 MW; 98D78F3E0F386F32 CRC64;
MTQHLVHRPA RATRPLPPAE ARTIEPPPNL PEGKMGSAAT ALLPMAGVMS SVVMMTVIRS
SQFAGLGAVV LVVALLGAVA LFLSQRGKAQ RQRRVQRERY LEYLEELREE LGAAERERRC
AARELNPPPS ALYDLVRDPS RLWERRRTDA DFLRVRVGVG DVPVQDVAVG QSSASGVLTP
PDPFMLNEAR ALQARFVTIA GHPLQVPLDR AGNVSVVGER EDVLQVARAL LVQASVTHAP
DDMALALGVP GESMSEWEWA KWLPHVLDPD TQDGPVAARR IAPDLAQLAR FLGADLKKRS
SYAAEVRRGL SDRTALSLGS RLLVVSDEYG ENAAELPRPD TAVDLGDMGV TVLHLLAERV
HEPDQVSVRI TVDGERVVVE DLRGERAVRV SGVLDPVGAG AAEGLARMLA PLRLSRESAA
EGTPVTGPVD FPELLGIGDP AALDLGRQWA RRGDRDFLRV PIGLDDRHEP VLLDLKESSE
LGMGPHGLCV GATGSGKSEL LRTLVLALVT THPPEDLAMV LVDYKGGATF APFTGLPHVA
GVITNLENQA GLVERVHTSL AGEIKRRQQV LKDAGNIADI GRYRALRDTG RPDLEPLPHL
FVVIDEFGEL LTAKPDFIDL FLSIGRIGRS IGVHLLLSSQ RIEGGKLKGL ETYLSYRLGL
RTFSADESRT VLETPDAFNL PPLPGFGYLK VDTSTYARFK AGFVSGAHRA PVPRDAAAAD
EPLAWAYPSY NTVATAAGAA GDDGAVAPRE RESGPTVLST VVEQLVGAAE PVRRIWLPPL
PDTVTLARAA GPVRASADGM QLAHRDGPLR VPLGVLDVPA RQWQGRWVHD LDTAGGHTAV
IGGPQSGKTT LLRTLALSLA LTHTPRDVAI YGLDLVGGGL SALSGLPHVG GIAGRADHER
AARTVAEVRG MLAEREAVFR EHGIDSVDQL RSLRAQGLLP GLGSTDVVLL IDGFGALRDE
FAELDDAVAE LLKRGSGYGI HVVAGMLRWN DVRIAGQSMF GSRIELRLND PADSSIDRKL
SETLSADTPG RALTDGRLFG HVALPRLDAL GSTADLAPAL EEAVRSLRAT WHGEPAAPVR
VLPTRLPAGR LPSTAAVPRA VPIGVDQDAL SPVVLDLFGA DQHLLVLGDN ECGKTNLLKL
ISRALVDRHG EDELVFGVFD PRRGLRGVIP EPYRGGYAHN AKLSAALATG IAAELEKRLP
ESADPDATND DPAFTGPRIV ILVDDYDILT TAGQQPLAPF LPYISSAQDI GLHFVVARRV
AGASRALYEP FLTTLRETGA TAFVMTGDRT EGQLFPGLYA SAQPPGRGTL VRRGRRHQLI
QTALAADTDP METPA
//
