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Database: UniProt
Entry: A0A2A3HTL0_9ACTN
LinkDB: A0A2A3HTL0_9ACTN
Original site: A0A2A3HTL0_9ACTN 
ID   A0A2A3HTL0_9ACTN        Unreviewed;      1322 AA.
AC   A0A2A3HTL0;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=S-DNA-T family DNA segregation ATPase FtsK/SpoIIIE {ECO:0000313|EMBL:PBC71092.1};
GN   ORFNames=BX265_5672 {ECO:0000313|EMBL:PBC71092.1};
OS   Streptomyces sp. TLI_235.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1938860 {ECO:0000313|EMBL:PBC71092.1, ECO:0000313|Proteomes:UP000218662};
RN   [1] {ECO:0000313|EMBL:PBC71092.1, ECO:0000313|Proteomes:UP000218662}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TLI_235 {ECO:0000313|EMBL:PBC71092.1,
RC   ECO:0000313|Proteomes:UP000218662};
RA   Klenk H.-P.;
RT   "Sequencing the genomes of 1000 actinobacteria strains.";
RL   Submitted (AUG-2017) 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:PBC71092.1}.
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DR   EMBL; NSGV01000002; PBC71092.1; -; Genomic_DNA.
DR   Proteomes; UP000218662; 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   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:UP000218662};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          462..661
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          815..1008
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1101..1285
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         485..492
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         1118..1125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1322 AA;  143842 MW;  609340CE886FC1A3 CRC64;
     MGVVLIKRKP RRPGPAMPDG EVQLQEPPGL PEKQSGMSSV LTMAPMALGS LSMVFMFLHP
     GGTQGGGALS YLAMGMMALS AVGMLLTQLI RGSSDRKQQL RAERRDYLRY LSQMRRQVRH
     SIDAQRLALA WRHPAPEELW TLVGTSRLWE RRLTHPDFSD VRIGLGTQRL ATPLAPLATK
     PVEDLEPLCA HALRRFIHAY GTVDDQPMAI HLRGFAHVLL RSDDPATARA MLRAVLAQLA
     VVHGPDELTV AVVTAVEQRA EWEWTKWLPH ALHPTDTDGA GPVRLVAGSL GEVEQLLGEE
     FTGRPGFEPD AAPERDEPFT VVVLDGPGAH TGSRAALAGY RNAVLIDLAD TLEWSPARTT
     LRLRIEDGRL TMVGSDSNRK DVVTDLGRPD ALALPAATRL AARLARYRIA DGVDAAEPLA
     TDFDLTALLG IADLNTLDVD ALWAQRGIPQ RLRVPLGLGP DGRPVDLDLK ESAQGGMGPH
     GMLIGATGSG KSELLRTLVL ALAVTHSSEV LNFVLVDFKG GATFLGLDTL PHTSAVITNL
     ADESSLVDRM RDALHGELVR RQELLRDAGY ASLLDHETAR AAGTVLRPLP TLFVVVDEFS
     ELLSAHRDFM ELFIMIGRLG RSLGVHLLLA SQRLDEGRMS ALESHLSYRI GLRTFSAMES
     RGVLGVPDAY QLPSQPGNGF LRSDISTLTR FKAAYVSGPY RPKRSAARQA AIAGQVVAYG
     TDYVMPRRPQ TSPVEPEEEQ GPVGSLLEVA TGRLHDAGPP AHRVWLPPLD VPPTLDELLP
     PLVPHPRRGL TTEHAGSHGT LRLPLGVVDR PFQQLRDLLI ADLAGAGGHV GVAGAPQSGK
     STLLRSLIAG LALTHTPAEV QFYCLDFGGG TLSTLRSLPH VGGVTGRHDG ERVLRTVAEV
     NTVITRRERY FAALGIDSVS DFRRRRAAGD LPEEEQHGDV FLVIDGWNTL RQEFNDLVQP
     LTLMSQRGLN YGVHLVIGTT RWGEIAGGLR DQLQTRFELR LGDAVDSVIN MRAATKVPKL
     PGRGLTEEQL HFLAALPRID GSGRTDDLGE GIADLVDAVV AHWSGPRAPG VRMLPLSLEA
     ERLPAPQGRL RVAIGLEDTE ISPLWHDFEE NPHLLVVGDT ESGKTNLLRL MIDAITTAYT
     PSQARIMLVD YRRGLYDAVP EEYRLGYAVA VDKVRQIVDG ASRAMKNRVP PADITPARLR
     LRDWWTGPEL FVLVDDYDLV GSGSGSHPFA ALLEYLSQGT EIGLHLVVAR GANGIGRGLA
     DPLLRKLQEV NSPALLMSCP PSEGYLFGNF KPRQLATGRG YYITRRRTVQ VQTGHIAEEG
     KD
//
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