ID   A0A1N7CLW0_9ACTN        Unreviewed;      1316 AA.
AC   A0A1N7CLW0;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=DNA segregation ATPase FtsK/SpoIIIE, S-DNA-T family {ECO:0000313|EMBL:SIR64591.1};
GN   ORFNames=SAMN05444858_113143 {ECO:0000313|EMBL:SIR64591.1};
OS   Micromonospora avicenniae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=1198245 {ECO:0000313|EMBL:SIR64591.1, ECO:0000313|Proteomes:UP000186004};
RN   [1] {ECO:0000313|EMBL:SIR64591.1, ECO:0000313|Proteomes:UP000186004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45758 {ECO:0000313|EMBL:SIR64591.1,
RC   ECO:0000313|Proteomes:UP000186004};
RA   Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FTNF01000013; SIR64591.1; -; Genomic_DNA.
DR   RefSeq; WP_076472147.1; NZ_FTNF01000013.1.
DR   STRING; 1198245.SAMN05444858_113143; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000186004; 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:UP000186004};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        66..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          456..656
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          814..1005
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1097..1281
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          95..122
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        12..30
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         479..486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         832..839
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1114..1121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1316 AA;  143165 MW;  6DC93505D8CBD7E3 CRC64;
     MSSLVVVKRP PRRPAPMLPT GEVLLDPPPE VPPAGGRGWT RMLMILPMAA GAAAMGLMMG
     MQRGGVMTYV VGGMYGVSIL GMIAVMVVNQ SGPGKKEMIE SRRQYMRRLA QLRAQVRATI
     RQQREALHYR HPDPDALWST ASSGRLWERR RGDADFGVVR IALGPQEVAT PLVPPQARPV
     DELEPLCALA LRRFVSTYSV VPDLPVAIAL RDFSHVYLRG EGDAVSGLVR AILAQMTSFH
     APEDLLVAFC VAEDRRAEWE WAKWLPHAQH PDKLDAVGPI RLFAPTVVAL EAMLVDVLSN
     RPRFDPAVTQ STLPYVLVVI DGGHVGGADH LMTEGGLAGV TVLDLTSRPP RLLDETSVVL
     DVAEDGSVSG TTADGTTRVG QADALGRDAI EVLSRELAPL RLSAVSYQEQ QAVNVDLGLA
     ELLGLGDPYE LDLTESWVNR PTRNRLRVPI GVNESGRPIE LDLKESAQEG MGPHGLLVGA
     TGSGKSELLR TLVLALAVTH SPEILNLVLV DFKGGATFAA MDRLPHTSAV ITNLSEELFL
     VDRMLGAIQG EITRRQELLR RAGNYASQRD YERARAAGVP LEPLPSLLIV VDEFSELLSA
     RPDFIDMFVQ IGRVGRSLGM HLLLASQRLE EGRLRGLETH LSYRLGLRTF SSMESRAVLG
     VADAYELPRS PGHGYLKAGT EGLIRFKAAY VSGAVRHQSG VPTVGGRQID PVRDYSTDYV
     PVVADEEPDE AVETPNEEFV GESLLDVLVE RMEGRGPAAH QVWLPPLDEP PTLDQLLGPI
     APIPQRGLTV AEEARHGALQ GVAGIVDKPL EQSRDPFWID LSGAAGNVMV VGAQQTGKSN
     LLRTLVTSLA LTHTPREAQF YCLDFGGGTL AALSGLPHVG GVANKREVDK VRRTIAELHG
     LMQARDAMFA TEGIEGAAGY RRARREGRFR QDPFGDVFLV VDGWSTLRAD FEDLEPMVTE
     LTNRGLGYGI HILATTNRWM DVRPAVRDMF GTKVELRLGE PADSVINRRA AVNVPEQHGH
     GLTPDGLHFL AGLPRVDGRQ ETDDLPDALG DLVKLIQQNW TAAGAPPVRL LPAELPYDSL
     PAAQGGVIPV GIAETNLQPV HLDFTAEPHL LLFGDVECGK STFLRTMARS IVSGNDPAKA
     RLILVDFRRS LLGAVDSEHL IGYGTSQQVT ADLVKQVVTV MKERLPGREV TQEQLRNRSW
     WKGPELYVLV DDYDLVAGAS VNPLGPLLEF LPQARDIGLH LILTRRIGGA SRAMFDPVIG
     RIRELASPAI MMSGPREEGA LFGNMKPQRL PAGRGWLFTR RGGAQLVQLP WLPPTQ
//