ID A0A0F7N6I6_9ACTN Unreviewed; 1642 AA.
AC A0A0F7N6I6;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Cell division protein FtsK {ECO:0000313|EMBL:AKH83008.1};
GN ORFNames=AA958_13090 {ECO:0000313|EMBL:AKH83008.1};
OS Streptomyces sp. CNQ-509.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH83008.1, ECO:0000313|Proteomes:UP000034283};
RN [1] {ECO:0000313|EMBL:AKH83008.1, ECO:0000313|Proteomes:UP000034283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH83008.1,
RC ECO:0000313|Proteomes:UP000034283};
RA Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA Kalinowski J., Heide L., Kaysser L.;
RT "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific Producer
RT of Meroterpenoid Chemistry.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP011492; AKH83008.1; -; Genomic_DNA.
DR RefSeq; WP_047016340.1; NZ_CP011492.1.
DR STRING; 444103.AA958_13090; -.
DR KEGG; strc:AA958_13090; -.
DR PATRIC; fig|444103.5.peg.2754; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000034283; Chromosome.
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 CDD; cd01127; TrwB_TraG_TraD_VirD4; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR002543; FtsK_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR22683:SF41; DNA TRANSLOCASE FTSK; 1.
DR PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR Pfam; PF01580; FtsK_SpoIIIE; 2.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50901; FTSK; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Cell cycle {ECO:0000313|EMBL:AKH83008.1};
KW Cell division {ECO:0000313|EMBL:AKH83008.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000034283};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 352..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 814..1007
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1150..1345
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 39..119
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 313..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..118
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 225..251
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 832..839
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1167..1174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1642 AA; 175705 MW; 1ACAB924018FE3ED CRC64;
MRLTLTVVDP LGGDRADVVL DAEAESSVGD VARVLAGQLD SPPPAAVPHG APQAAQVPAS
HAQQAQHAHA QAAPAQMPGG WATAGAPPAA PPGSPPAAVP FGAPGAPPQQ PAAAPAPPPV
FVDGFAVDPR LPVAQSPLRE GTVVSLYDPV GCPPREVTGL VELRVVGGPM AGAVHRLGLG
RVDVGSGNAT HIRVSDPELP ERAFSLTVSA DGTCKVHVHG DQEKATLDGT TFAERAKPKE
KSDDDDTRRA RRRRRREARR EERRRRRAGE PAPPPLPQEP PQSKDAWPYG AQVAMGNSLF
ELVRYAPPDA AVATSEDGAG LDYNRPPRLL PPDRETRFKL PAPPKEGQAR PLPWLMALMP
AVMGVTMCLV MGRWYYLLMA FMSPIIMIGN YFMDKKHGRK SHVKAVAEYK EHKARIEKDA
RDALVAERNE RRLGGPDPAL LLSTATGPRT RLWERRRTDA DHLLIRFGTA ELDSEVLLED
PEQDEHRRQV LWKIQDAPVT VPLRQIGVLG IAGAGDTPRS LGRWAVAQSA VLHSPLDVQF
YVLTEPGGQA GWDWMRWLPH ARPAGEYDTN ALIGTDTETV AARIAELTQL LDARQKAAKD
QRSSGPTSFK DPDIVIVFDG SRRLRSLPGV VRLLREGPAV SMFAICLDSE DRFLPGECQA
IVVAEPKPEE HDPRAAAAQG IPLQQVAGAG GPGGPGGYPP FQVGAWGNGQ AQDAAQRAAA
ADGTGPIRLR VEQAGSERRR GVRPDFVSPA WCALVARGLS PVRDISGEAE DAAIPSSSRL
LDVVELEPPT GDAIAARWQI GGQSTTAVIG ESYDGPFAID IRKDGPHGLI AGTTGSGKSE
LLQTIVAALA VSNTPENMTF VLIDYKGGSA FKDCVKLPHT VGMVTDLDNH LVTRALESLR
AELHRREHIL ADAEAKDIED FQDLLRREPG RYAPLPRLLL VIDEFAAMVR ELPDFVTGLV
DIAARGRSLG IHLMLATQRP SGVVSPEIRA NTNLRIALRV TDGGESADVI DAPDAGFIAK
SMPGRAYVRL GHASLVPFQS GRVGGRRPGA ADPATAQPWA GRLGWAELGR GALKRPAGAQ
QEEDEITDLK VLVDAVNEAN ERLGIPEQHS PWLPALPDSI ELDALPAPQG AGPLPPAPYG
IEDLPAQQAR RTVAIDFADF GHLIVGGAPR SGRSQMLRTI AASLARTHSV ADLHLFGIDC
GNGALNALTR LPHCGAVVSR NQTERAVRLI GRLKQELGRR QELLAADGFA DIAEQRAAAS
DPEQKLPYTV VLLDRWEGWL PTLGEINHGD LTDEIYGLLR EGASVGIHMI ITGDRSVLTG
RISTLTEDKF AFRLPDRSDF SMISLNARNI PEDIAPGRMF RAESGLETQI AVLSDDLSGA
AQAAAVAAIG EAATARDAAV PRSLRPFRVD VLPSRLGFEE AWEMRDVQAQ EASKLWALVG
VGGDELMGFG PDLADGIPAF IIGGPAKSGR STVLKAMALT FLQQGVRLVI AAPRPSPMRE
LADREGVLQV FTEDDIDEDE VHDLLRQASP DEPIVVLVDD AEMLTNCDAG DEFKAIARRG
AERGWALVLA GDEEEVASGF SGWQVEAKKA RRGVALSPQD PSAGDLIGIR LNRGSVGDQV
QPGKGLLHLG DGEPFAVTTP LT
//