ID   A0A1C3N9C2_9ACTN        Unreviewed;      1331 AA.
AC   A0A1C3N9C2;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SBV29171.1};
GN   ORFNames=GA0070620_4741 {ECO:0000313|EMBL:SBV29171.1};
OS   Micromonospora krabiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=307121 {ECO:0000313|EMBL:SBV29171.1, ECO:0000313|Proteomes:UP000199393};
RN   [1] {ECO:0000313|Proteomes:UP000199393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45344 {ECO:0000313|Proteomes:UP000199393};
RA   Varghese N.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT598496; SBV29171.1; -; Genomic_DNA.
DR   STRING; 307121.GA0070620_4741; -.
DR   PATRIC; fig|307121.4.peg.4838; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000199393; 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:UP000199393};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        65..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          475..675
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          830..1024
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1113..1297
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..26
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         498..505
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         849..856
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1130..1137
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1331 AA;  142163 MW;  83C919A207B207F1 CRC64;
     MSTVVIKRPP RRPAPEIPAG ELPVEPPPEI PVGTGGRWQQ LLMVLPMLGG TVAMAMMFGR
     GGGAYAYLVG GMFGLSSLAM LVTSWGSASG TPRKSEMMAA RREYLRHLAG LRRRVRQTAG
     QQRDGLYYRH PDPGRLWSTV ASHRVWERRP ADPDFAVVRV AVGPQTLATP LVPPVTRPLE
     ELEPMTAGAL RRFLDAYSVV PDLPVALSLR SFARVFVAEA PTVGAATVDD GRPAVDGGPA
     RGQAARALVR AVLTQLAVFH APDELLVAVC AGPERRAAWE WVKWLPHVHH PTRTDALGPV
     RLVASSATDL ERLLDDVLGN RSRFSPTGAA TDGPHVVVVL DGGDLTGATD LTGDGGIDAV
     TVLDLDTPPP RLLDRYALLL ELRDGRLHSY SVEGRAEVGV PDRLEPADAE AVARRLAPLR
     LAGAARGPDA PLATDLGLPD LLGLGDPEGF TVEQGWAPRS ARERLRVPIG VGADGGAIEL
     DLKESAQDGM GPHGLLIGAT GSGKSELLRT LVLGLAATHS SEQLNFVLID FKGGATFASF
     DRLPHTAAVI TNLADALPLV DRMVDAINGE LVRRQELLRR AGNFASVRDY ERARAAGSPL
     APLPSLLLIC DEFSELLSAK PDFIDLFVQI GRLGRSLGVH LLLASQRLEE GRLRGLDTHL
     SYRIGLRTFS ALESRTVLGV PDAHDLPRTP GHGYLRFGTE PLVRFRAAYV SGALPRHGPA
     AGSGAGGARR LLTFTTHLVP VPEPTTTPPP ETAEADSRGS LLDLLVDRLA GQGPPAHQVW
     LPPLDRPPAL DELLGPIVVD PARGLTTANP ELHGALGVPV AVVDRPFEQR RDLLWLALDG
     AAGHVAVVGA PQSGKSTLLR TLVCALALSH TPAEAQVYCL DFGGGGLAAL RELPHVGGVS
     GRADPTAVRR TVGEVATLLA ERERRFAELG VESMAAYRRR RATATDQPTS DPFGDVFLVV
     DGWTTLRAEY DDLEPLITDL ATRGLSYGVH VVTTALRWLD FRPAIRDLFG SRLELRLGDP
     ADSLVARRAA ANVPEKFPGR GVTAESLHFL TALPQLAGST ADTAGLVKQV AEAWPGRPAP
     RVRLLPPVLP YAELDLTAAA GLRLPVGIAE ADLRPVALDF AVEPHFVVFG DAECGKSSFL
     RALATTIVTR FTPEQARVIL VDYRRSLLGA IESPHLIGYG TAAAHTADLV ESAAGYLARR
     IAGPEVTPQQ LRDRSWWSGP ELFVLVDDYD LVATGPTNPL RALEEYLPQA RDVGLHLVLV
     RRSGGAGRAQ YEPIVQRLRE LSTAGLVMAG NPEEGALVGP ARPGPLPPGR GRLVTRREGV
     RLVQLAHLPP S
//