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Database: UniProt
Entry: A0A1H2C7K0_9ACTN
LinkDB: A0A1H2C7K0_9ACTN
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ID   A0A1H2C7K0_9ACTN        Unreviewed;      1323 AA.
AC   A0A1H2C7K0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SDT66498.1};
GN   ORFNames=SAMN04489716_5357 {ECO:0000313|EMBL:SDT66498.1};
OS   Actinoplanes derwentensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=113562 {ECO:0000313|EMBL:SDT66498.1, ECO:0000313|Proteomes:UP000198688};
RN   [1] {ECO:0000313|EMBL:SDT66498.1, ECO:0000313|Proteomes:UP000198688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43941 {ECO:0000313|EMBL:SDT66498.1,
RC   ECO:0000313|Proteomes:UP000198688};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT629758; SDT66498.1; -; Genomic_DNA.
DR   STRING; 113562.SAMN04489716_5357; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000198688; Chromosome i.
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   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   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; 3.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 3.
DR   PROSITE; PS50901; FTSK; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000198688};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          456..655
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          811..1003
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1100..1282
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          710..735
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         479..486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         829..836
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1117..1124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1323 AA;  144607 MW;  66B97DC189C66BBF CRC64;
     MGTTPYSRKA RRAGPVAPAE EIALQEPPII PEPAERGISA VLMLAPMAIA SLAMVLMFLR
     PNAGALAYVG VMLMVLSAVA MMIVPIIRNA GQHKHRLNGE RRDYLRYLGQ VRRKVRGSLT
     EERRAARWLH PDPGALWSMA LSQRLWERRT AHADFGEVRL GLGARRSTTR LVAPSSKPVE
     DLEPMAAHAL RRFLRAYSTM QDAPIAIYLR GFSRIGFQGD LNTTRSAVRA MLAQLVVAHS
     PADLYLVLVT TGPHWDWAKW LPHVQDDSAP DVTGTRRRFV TDLTQLDEAL AVLGVPERPG
     YEPDTPVTAI EQYVVVVLDW PLLPSGHRLG AEGYRNVVTL DIGATLGWEP HPHTLLVQAD
     ESQLNITSFD HLGKSSSSPL CRPDRMGTVA AGALARSLAR YRVGAGGDTE EPLATDYDLA
     GMLQLGDLTR FDTAAYRSGR SPAQRLRVPI GMTSTGMQIE LDIKEAAEGG MGPHGMLIGA
     TGSGKSELLR TLVLALAARH SSEDLNFVLV DFKGGAAFVG FERLPHTSAV ITNLSEELEL
     VDRMQDALTG ELNRRQEHLR ASGYPSRREY ERARSEGTAM DPMPALFIVV DEFSEMLSSK
     PEFIDVFAMI GRLGRSLGVH LLLASQRVDE GRIHTIEGHL SYRIGLRTFS SMESRSVLGV
     PDAYELPNAP GNGYLRPDTT TLIRFKAAYC SGPWRPPHQR RRQSAQGGLV PFGTEHLVPD
     EPATPDEDAE PDSANEKAPV MADVLLEALR GQGPAAHQVW LPPLTDSTTL EKLLPPLVEH
     PTLGLAPVGG YGTGQLTVPI GLVDLPAQQR RELLTASLAG SAGNVGVVGG PQSGKSTLLR
     TLITALALTH TAAEVQFYCL DFGGGALASL ARLPHVGGVT GRLDRDKVTR TVLEVTNLLA
     HREQIFSQNG IDSMTSYRRA RRTGAFQDVD PYGDVFLIVD GWYTARQDFQ ELDDRFGEIA
     ARGLGFGVHL VVSAGRWTEI RPWLRDVLGT RFELKLGDPV ESEVHSRTAA TVPNIPGRGI
     TADRQHFLGA LPRIDGNPDT EDLAEATAEL VESLDVPSAP RAPLVKLLPD RLPVTMLPAA
     TAPSKEAEIR IPLGLDDVRL EPLWHDFDAN PHLLIFGDTE TGKTNLLRHI ARSIAAHHTP
     KEARIVFGDF RRELHDAIPQ VHQIGYSMSA ERLAATMAEA GQILTGRLPG PEIPPSRLAK
     RDWWTGGRMF ILVDDFELIE SGRDSPLAPL LPLLPHGAEI GLHLIIARST SGANRGMMNP
     VLRRAWDLGS PGLLLSCPRE EGSFLGNVKP RVLPVARGQY IDRRRSVRLV QTPEVPMPER
     PED
//
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