ID   A0A285LWF3_9NOCA        Unreviewed;      1347 AA.
AC   A0A285LWF3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SNY87986.1};
GN   ORFNames=SAMN04244553_4946 {ECO:0000313|EMBL:SNY87986.1};
OS   Nocardia amikacinitolerans.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC   Nocardia.
OX   NCBI_TaxID=756689 {ECO:0000313|EMBL:SNY87986.1, ECO:0000313|Proteomes:UP000219565};
RN   [1] {ECO:0000313|EMBL:SNY87986.1, ECO:0000313|Proteomes:UP000219565}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45537 {ECO:0000313|EMBL:SNY87986.1,
RC   ECO:0000313|Proteomes:UP000219565};
RA   Ehlers B., Leendertz F.H.;
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; OBEG01000005; SNY87986.1; -; Genomic_DNA.
DR   STRING; 1379680.GCA_001612615_02906; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000219565; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000219565};
KW   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   DOMAIN          461..661
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          825..1024
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1129..1313
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         484..491
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         1146..1153
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1347 AA;  146889 MW;  BCBEF292FC157718 CRC64;
     MSTVRFQRRA RREMPRTPGG EVTLQPPPEI PRVTPGNLLM KLMPVVMIIG MVGMMALLFT
     QGGGIASNPM SMMFPIMMLF SMVGMFAGQG GGKGQKAAEA NEDRKDYLRY LDQVRKDVDE
     TAKQQRASVE WSHPEPGLIW MLAGTSRMWE RRAGDKDFCH ARIGIGGQRL ATRLVAPETG
     PVEELEPIAA VSLRRFVRAH STVPDLPTAI AVKGFATIAL DGDRNEARDM VRAMLLQLCM
     FQGPDQVLVA VVCGPDTARE WEWTKWLPHT QHPDAQDGIG TQRMFYGSIR EATASLHPLL
     ANRVRYSRNQ PANAGLVQVV IVVDGGLLEA EDDQLRESGY EGVTIIDLCG YAPRLAVSRG
     IKMVVENGEC VGRGATGNQE RFALIDRISA HQAQQAARRL APYRAATQRS SDVETEDTEV
     ISTWAQLMSL GDIGSFNPES AWRPRYGRER LRVPFGVDAA GLPIELDIKE AAENGMGPHG
     LCIGATGSGK SEFLRTLVLS LLATHSPDQL NLVLVDFKGG ATFLGLEGVP HVAAVITNLE
     EEADLVDRMK DALAGEMNRR QEVLRQAGNF ANVSEYEKAR AAGADLDPLP ALFVVLDEFS
     ELLTQHPDFA ELFVMIGRLG RSLHVHLLLA SQRLEEGKLK GLESHLSYRI GLKTFSANES
     RQVLGVPDAY NLPNTPGGGY LKSDSGEIQR FQASYVSGPY VGGGSQREVT QAGVAGGEID
     VKARPFTAHH VDFRAIDRVP LPTQANHEPE EHRTEEGEQI SNLNMLVSRI RGHGRPAHEI
     WLPPLDEAPT LDQLIPRSIL TGEYSAVATL RAPIGIVDRP YDQRRDPLVV DLSGSRGNVA
     VVGGPQSGKS TALRTMIMAM SMTHTAEQVQ FYCLDFGGGT LASLEGLPHV GSVASRLDED
     KVRRTIAEMT TIVRQREARF RQLGIESMAE FRRLRSMDPS SSPAAAGAHE DPFGDVFLVI
     DGFGSIRQDF DPLEQPIMNL AVQGLSYGVH VVIALARWAE ARPALKDQIG TRIELRLGDP
     MDSDLGRKFA AQVPMGRPGR GMTPDCLHML TGLPRIDGSS DPTMLGQAVA DAVATIARLT
     PGRHAPAARM LPEVLPREQL LQLAGNWPSL LNSGVKNVRI PLGINESELA PVYLDFNESP
     HFIIIGDSES GKTTLLRSII EGIAAANSPN EARFILGDYR RTMLGLVPDG YLAGYGSTAP
     QFTQNMNDLA AYVAQRTPGP DVTPQQLRER SWWNGPELYV IVDDYDLVAT SMGNPVSALV
     EHLPHARDLG FHLIVARRAG GASRAMYEAT MARMKDLGSA GLIMSCPKDE GVLMGTVRPS
     PLPPGRGTYI TRNAQELIQL AWMPAAE
//