ID   A0A0A6WXI2_ACTUT        Unreviewed;      1312 AA.
AC   A0A0A6WXI2;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Secretion protein EccC {ECO:0000313|EMBL:KHD72402.1};
GN   ORFNames=MB27_38685 {ECO:0000313|EMBL:KHD72402.1};
OS   Actinoplanes utahensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1869 {ECO:0000313|EMBL:KHD72402.1, ECO:0000313|Proteomes:UP000054537};
RN   [1] {ECO:0000313|EMBL:KHD72402.1, ECO:0000313|Proteomes:UP000054537}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL 12052 {ECO:0000313|EMBL:KHD72402.1,
RC   ECO:0000313|Proteomes:UP000054537};
RA   Velasco-Bucheli B., del Cerro C., Hormigo D., Garcia J.L., Acebal C.,
RA   Arroyo M., de la Mata I.;
RT   "Draft genome sequence of Actinoplanes utahensis NRRL 12052.";
RL   Submitted (OCT-2014) 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:KHD72402.1}.
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DR   EMBL; JRTT01000137; KHD72402.1; -; Genomic_DNA.
DR   RefSeq; WP_043533070.1; NZ_JRTT01000137.1.
DR   STRING; 1869.MB27_38685; -.
DR   eggNOG; COG1674; Bacteria.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000054537; 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; 2.
DR   SMART; SM00382; AAA; 2.
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:UP000054537};
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..998
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1092..1276
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
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         1109..1116
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1312 AA;  142438 MW;  85903AC21E684BF1 CRC64;
     MGTVVIKRAA RRPAPEIPSD QLVVEAPPEI PEQVTGRWQQ WLMALPMLGG TMAMAMMMGQ
     GQRGAFSYVI GGLFGISSLA MLVTSFGASG GPRKAEMMAA RREYLRHLAS LRKRVRETAR
     LQRTGLIYRH PDPERLWSTV DSHRVWERRA ADPDFGVVRV GLGPQTLATP LIPPVTRPLD
     ELEPMTAGAL RRFLDAYSVV PDLPVAMSLR GFSRIFLRGE APGAEGPRAL VRAVLTQLAV
     FHAPEDLVIA VCAGQDARAH WEWVKWLPHA RHPSRTDALG AVRLVAEDEL ELARMLEDVL
     GNRPRFHPGE SAGSTPHVLV VIDGAEPANT RLDDALDGLT VLDLDTVPPR LLDRSTLVLQ
     VRADGVLGTW TMDHESEAGR ADGLTVAEAE AVARRLAPLR LATTVDPVSG TPTQTEAGLP
     ELLGIGDVEN FSVTHGWPAR PDRDRLRVPI GVSSDGLPVE LDIKESAQDG MGPHGLLIGA
     TGSGKSELLR TLVLALAATH SSEQLNFILI DFKGGAAFAS MDQLPHTAAV VTNLENALPL
     VDRMADALEG EMSRRQELLA KAGNYASLYD YERARAGGAP LAPLPTLFIV CDEFTEMLKE
     KQDFIEIFLQ IGRLGRSLGV HLLLASQRLE DGRLRGLDTH LSYRIGLRTF SALESRAVLG
     VPDAYELPKA PGNGYLKFGT EPMSRFKAAY VGGTVRRAGR SRGSARHDGP RVQAWSTRYV
     AAPVAAPEPQ PAPEQEDGPK LADVVIEKLV GQGPPAHQVW LPPLDESAML DELVGPVAVV
     PGRGLTFTNP SIRARLQVPI AIIDKPREQL RDVMWLNLAG AAGHLAVVGG TLSGKSTALR
     TLICGLALTH TPAEVQVYCL DFGGGSLGTL RDLPHVGGVF GRLDTAGVRR TVGEITTLLT
     EREARFADLG VDSMASYRSR RPANDPFGDV FIVVDGWGTL RKEFEELEPI LTDVATRGLS
     YGIHLVAATS RWLDFRAAVR DLFGSRLELR LGDPSESVAG RRAALDVPEG KPGRGMVQHP
     TDRNKGLHLL TVRPEVSTLG DTAGLVKAVA AVWDGAPAPR VRLLPMLVPY ADLHAERGHG
     LRIPIGINEA DLKPVEIDFA TEPNLVVYGD LESGKTSLLR SIATTLTSRF RPDQARIMLV
     DYRNSLLDLP ESDHRIGYGM EHGHTEKLMR SVAAYMAERK PGPSVTVQQR RDRSWWSGPE
     LFILVDDYDV VSSGATNPLE PLMEYLTFAR DIGLHLIVTR RTAGASSSMY RGILQQLKND
     SAAGLVLSGS PDEGALVGNV KPIPMPPGRG RLVTRREGVR MIQLAHQPPF EH
//