ID   A0A372G319_9ACTN        Unreviewed;      1311 AA.
AC   A0A372G319;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Type VII secretion protein EccCa {ECO:0000313|EMBL:RFS47100.1};
GN   Name=eccCa {ECO:0000313|EMBL:RFS47100.1};
GN   ORFNames=D0Q02_08095 {ECO:0000313|EMBL:RFS47100.1};
OS   Micromonospora craniellae.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=2294034 {ECO:0000313|EMBL:RFS47100.1, ECO:0000313|Proteomes:UP000262621};
RN   [1] {ECO:0000313|EMBL:RFS47100.1, ECO:0000313|Proteomes:UP000262621}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LHW63014 {ECO:0000313|EMBL:RFS47100.1,
RC   ECO:0000313|Proteomes:UP000262621};
RA   Li L., Lin H.W.;
RT   "Verrucosispora craniellae sp. nov., isolated from a marine sponge in the
RT   South China Sea.";
RL   Submitted (AUG-2018) 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:RFS47100.1}.
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DR   EMBL; QVFU01000005; RFS47100.1; -; Genomic_DNA.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000262621; 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:UP000262621};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        65..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          810..1006
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1093..1277
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..20
FT                   /note="Disordered"
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         829..836
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1110..1117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1311 AA;  139894 MW;  E068E7A7EAFE70D7 CRC64;
     MSTVVVRRPT RRPAPEIPVG EVPVQAPPEI PAVTGGRWHQ MLMVLPMLGG TVAMAMMFGR
     GGGAYAYVVG GMFGLSTLAM LVTSWGSASG SPGKAEMMAA RREYLRHLAT LRRQVRETAA
     RQRNGLCYRH PDPTRLWSTV ESHRVWERRP ADPDFAVVRV AVGPQTLATP LVPPVTRPLE
     ELEPMTAGAL RRFLDAYSVV PDLPVAVSLR SFARVFVQAG PAGAPAAQSL VRAMLTQLAV
     FHSPDELLIA VCAGPERRGV WEWVKWLPHA GHPSRGDALG PVRLVASAAV ELEKLLDEVL
     ASRSRFSPAG PATDGPHLVV VLDGGDLTGA TELPGDGGID AVTLIDLSSP PPRLLDRFAL
     LLELRGGRLH SHSADGPVEV GTADALGIAE AEAVARRLAP MRPAVARGPD AATGAEPGLP
     ELLGIGDPEG FTTEQGWAPR SARDRLRVPI GVGVDGAAVE LDLKESAQDG MGPHGLLIGA
     TGSGKSELLR TLVVGLAATH SSEQLNFVLV DFKGGATFAS FDRLPHTAAV ITNLADALPL
     VDRMVDAING ELVRRQELLR RAGNFASLRD YERARAAGTA LAPLPSLLLV CDEFSELLSA
     KPDFVDLFVQ IGRLGRSLGV HLLLASQRLE EGRLRGLDTH LSYRIGLRTF SSLESRTVLG
     VPDAYELPRS PGHGYLRSGT EPLLRFKTAY VSGAVRRHAA TAGAPGSDRS RLLTFSTHFT
     PDPEPPATPT TEDEEPGRET LLEMLIGRLA GQGPPAHRVW LPPLDGAPGL DELVGLLTVH
     PARGLTSDNP ELHGALQVPV AVVDKPYEQR RDLLWLALDG AAGHVAVVGG TQSGKSTALR
     TVICALALTH TPAEVQVYCL DFGGGGLAAL RDLPHVGGVT GRADPTGVRR TVGELATLLA
     DRERAFAELG VESMAAWRRQ RVERAAEGTP DTDRFGDVFL VVDGWTTLRG EYDDLEPLIT
     DLATRGLSYG VHVVATAVRW LDFRPAIRDL FGSRLELRLG DPSDSLVARR AAADVPERTP
     GRGVTAGSLH FLTALPQVAD ADTATLVQRA AKGWSGPPAP RVRLLPAVLP YAELDLAATA
     GLRIPVGIAE ADLRPVVLDF VTEPHFVVYG DAECGKSSFL RALAQSIVTR FTPEQARVIL
     VDYRRSLLGA IETEHLIGYG TAAAHTADLV ESAAGYLQGR TPGPEVGPAQ LRDRSWWTGP
     ELFVLVDDYD LVASGPANPL RALEEHLPHA RDVGLHLVLV RRCGGAARGQ YEPVVQRLRE
     LSTSGLVMSG SPEEGALVGA VRPGPLPPGR GRLSTRREGV RLVQLAYLPP Q
//