ID   A0A1R3UJP0_9ACTN        Unreviewed;      1334 AA.
AC   A0A1R3UJP0;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=FtsK/SpoIIIE family protein, putative EssC component of Type VII secretion system {ECO:0000313|EMBL:SIO86109.1};
GN   ORFNames=BQ8420_10330 {ECO:0000313|EMBL:SIO86109.1};
OS   Nocardiopsis sp. JB363.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1434837 {ECO:0000313|EMBL:SIO86109.1, ECO:0000313|Proteomes:UP000195722};
RN   [1] {ECO:0000313|EMBL:SIO86109.1, ECO:0000313|Proteomes:UP000195722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JB363 {ECO:0000313|EMBL:SIO86109.1,
RC   ECO:0000313|Proteomes:UP000195722};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FRFF01000065; SIO86109.1; -; Genomic_DNA.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000195722; 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; 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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000195722};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        64..85
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          467..667
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          825..1016
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1111..1293
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          712..755
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          98..125
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        13..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         490..497
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         843..850
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1129..1136
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1334 AA;  146876 MW;  CE82AAA5AA4753F3 CRC64;
     MALRVVHRPT RTTHPAPAEE SREVEAPPTL PDGKSQGNPL MAILPMVGMM ASLTIMMVMR
     NPAFMALGAV VLCVALLGAL LMLFSRRGQV GRQRRNQREL YLQYLEELRE RLSVWEQETR
     AHARLLDPPP EALYDVLRDP KRLWERRRRH HDFLKVRVGT GVASGRPLNL AEQGTALAPT
     DPFMQSEAEG VIQRFATIPD MPFTLPLDMT GNVSVVGERE DIMRLVRAMV AQFAVFHAPE
     DAGLAVSYPE EHADDWSWLL WLPQVLDPQR RERGVATRLI ARSPRDLGTL LADELRSRSD
     FASEVRRGMG RREAYQMLRR LLVVHDTHGE VATELVRPDH TVDPTSLGVT VLHLVSRQID
     EPGDVNVRIT VTGDQIRVED LRPTDPVVRT GVLDDVSPAT LTGLSRMLSP LRLSAESIEE
     TAQEGGRVDF TAMLGVRDPG DMDVQRLWAP RSERAFLRVP IGVDEMGQAL VLDLKESAQL
     GMGPHGLCVG ATGSGKSEML RTLVLALAAS HPPERVSMVL VDYKGGATFA PFEDLPHVSG
     MITNLEDDAA LIERVHASLS GEVQRRQQML RDAGNVPNIG DYTYKREKDP SLDPMPHLLV
     IIDEFGELLT ARPDFIELFL SIGRIGRSIG VHLLLSSQRI EGGKLRGLDT YLSYRLGLRT
     FSEEESRTVL NTPDAFHLPA LPGFGYLKVD TTVYQRFKAG YVSGAYRGPV IEEEPEDENA
     TPSPRLYTAY NPSPEEVAET ATPEEETSMP SRTTDPTLLD VMVGQLGQHG EPTRAIWLPP
     LPKATTIDAI CGAPEETEHG LRIPGERPAL HVPIGLLDDA TKQWQGEWLL DLTASGGHVA
     IIGGPQSGKT TLLRTLVLSL ALTHTPDQVS VYCLDLLGGG LQSLSGLPHV GGVAVRTDAE
     RVRRTLEEVR GMLEHREEVF RERGIDSMEQ LRAMHARGEV PELATADIVL CVDGFGTLRR
     DFEEVEGIVT ELLQRGGGYG VHIVSAMLRW NDVRMNAQSN FGQKVELRLN NPTDSAIARK
     LAETIGEGDN GRALTPMKLF AQTALPRFDG APSTENLGDV VERAVRAIDR AWMGTRAPEV
     RVLPHRLSVL SLPDKEAEPK TLPIGLDERA MAPVRLDLFE RDQNLLVIGD SECGKTNLLR
     MIAEGLVERY TPKEVVFAIM DPRRNLRDVV PPEYVGGYAT NPRVCGGLAT GVAKEMENRI
     PQDGEGQEVE PGAFEGPRVV VLADDYDVLT TAGQKPLSPF VPYVSNGRDI GLHFVIARRA
     AGASRGMYDS LLQAVREVGS STLLMSGDRG EGQIFPRVYA SPLPTGRGKW MPRGGATRLI
     QTALLDQDRP ADHA
//