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Database: UniProt
Entry: A0A1C4UTP5_9ACTN
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ID   A0A1C4UTP5_9ACTN        Unreviewed;      1321 AA.
AC   A0A1C4UTP5;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SCE74992.1};
GN   ORFNames=GA0070612_0737 {ECO:0000313|EMBL:SCE74992.1};
OS   Micromonospora chokoriensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=356851 {ECO:0000313|EMBL:SCE74992.1, ECO:0000313|Proteomes:UP000198224};
RN   [1] {ECO:0000313|EMBL:SCE74992.1, ECO:0000313|Proteomes:UP000198224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45160 {ECO:0000313|EMBL:SCE74992.1,
RC   ECO:0000313|Proteomes:UP000198224};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT607409; SCE74992.1; -; Genomic_DNA.
DR   eggNOG; COG1674; Bacteria.
DR   Proteomes; UP000198224; 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; 3.
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; 2.
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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..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          455..655
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          816..1007
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1103..1287
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          9..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         478..485
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         834..841
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1120..1127
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1321 AA;  143110 MW;  DB55DCDDE5467B9E CRC64;
     MSTVVFRRLP RQPGPALPRG EVLLESPPEL PEPTPRGMGQ LLMILPMFCG VGAMAFLYAG
     KGGGMMTYVA GGLFGVSMLG MAIGSLANSG GKDKAELNAD RRDYMRYLAQ MRKRTRRAAE
     QQRAAMAWRH PEPDALWSIA ASRRLWERRI TEDDFGETRI ALGPQRLAVE IVPPETKPVE
     DLEPMSAIAL RRFVRAHSTV PELPTALSVR AFSRVVLRGD REPVLSLTRA ALGQLATFHA
     PDDLVVAVVA APDRQSSWDW VKWLPHAHHS ARTDAAGARR LVFASLAEAE AALAGELAAR
     PRFAPEAKPL TTAAHLVVVI DGGEVSPTCQ LVGPGLLGTT VIDLSGTVPR DAGRWLLCLD
     VADGSSLDLV RGSSSSPLGR PDQLSAEAAE GLARQIAPYR LSQQQTSNEE PLARSMELPD
     LLGVGDAATL DVQNTWRPRG HRDRLRIPLG VGPDGNVVEL DFKESAHEGM GPHGLVIGAT
     GSGKSELLRT VVAALAVTHS SEELNFVLVD FKGGATFASL EALPHTSAVI TNLADELPLV
     DRMRDALAGE MVRRQELLRA AGNYVSRFEY EKARAAGEPL APMPSLLIIC DEFSELLAAK
     PDFIDLFVMI GRLGRSLGVH LLLASQRLEE GKLRGLDTHL SYRIGLRTFS AVESRIVLGV
     PDAYELPNAP GHGYLKTDTS TMLRFRAAYV SGAYRAPGQQ ASASQALVQR RIVPYGLDFV
     PAQLPQMPVA AAPEPEQPAD GKAVAMLDVL IDQLKGRGRP AHQVWLPPLA DPPGLGELLG
     ALAVDPTYGL CTASWPGRGR LTVPVGVVDR PYEQRRDPMM VELAGAGGNV VIVGRSLSGK
     STMLRTLLAS LALTHTPREV QFFCLDFGGG ALRSLERLPH MAGVAGRRDV EAVRRTVAEV
     VAVLDDRETR FAQHGIDSVA SYRRRRAAGE FVDDPFGDVF LVVDGWNTLR QEYEELEQTI
     TTLANRGLGF GVHVVLTAVR WAEIRINMRD LLGTKLELRL GDASESEIDR RAATNVPEKS
     PGRGLTRDKL HFLTAISRID GRRDIDDLSE ASVSLAGHVA ANWPGRPAPK VRLLPRRLPV
     GELARIIDRS APGLPIGVNE SALAPVYLDL VNEPHLTVFG DAECGKTNLL RLIARGITER
     YTPAQARLVI ADYRRGLLGA VEGDHLLDYA PSNQAFAQGL ASIRSALSNR LPGPDVTTAQ
     LRDRSWWKGP DLYILVDDYD LVASGGSNPL SALQELLPQA RDIGLHLIIT RRVGGVSRAL
     YEPVLQRLRE LDSPGLLMSG SREEGAVFGT LRPSPQPPGR GTLVRRRDGQ QLIQTAWAEP
     A
//
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