ID   L7FG19_9ACTN            Unreviewed;      1326 AA.
AC   L7FG19;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Type VII secretion protein EccCa {ECO:0000313|EMBL:ELP70016.1};
GN   Name=eccCa {ECO:0000313|EMBL:ELP70016.1};
GN   ORFNames=STRTUCAR8_02450 {ECO:0000313|EMBL:ELP70016.1};
OS   Streptomyces turgidiscabies Car8.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=698760 {ECO:0000313|EMBL:ELP70016.1, ECO:0000313|Proteomes:UP000010931};
RN   [1] {ECO:0000313|EMBL:ELP70016.1, ECO:0000313|Proteomes:UP000010931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Car8 {ECO:0000313|EMBL:ELP70016.1,
RC   ECO:0000313|Proteomes:UP000010931};
RX   PubMed=21087627; DOI=10.1016/j.plasmid.2010.11.002;
RA   Huguet-Tapia J.C., Badger J.H., Loria R., Pettis G.S.;
RT   "Streptomyces turgidiscabies Car8 contains a modular pathogenicity island
RT   that shares virulence genes with other actinobacterial plant pathogens.";
RL   Plasmid 65:118-124(2011).
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:ELP70016.1}.
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DR   EMBL; AEJB01000110; ELP70016.1; -; Genomic_DNA.
DR   STRING; 85558.T45_03439; -.
DR   PATRIC; fig|698760.3.peg.1329; -.
DR   Proteomes; UP000010931; 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; 2.
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:UP000010931};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..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          459..659
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          815..1006
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1102..1287
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   BINDING         482..489
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         833..840
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1119..1126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1326 AA;  144618 MW;  88FC26A45D1916BA CRC64;
     MSVVLFRRPA RRRGPDMPEG ELTLQEPPTL PEVVADSSAI WTYLPMAMMS VSMMLMFIRP
     GGGNGAFMYI ALGMMVLASA AMMVGQVMRK AGERKERLRG ERRDYLRYLT QTRRKVHRAV
     VEQQLALAWR HPDPKVLRTM VRTTRLWERR VKDEDFGEVR IAVGDQQFAM RLNPLSTKPV
     EDLEPLSAHA LRRFVRAYST VPEQPIALYL RSWSRVLTRG DDAAVRAMVR AALCQLALFH
     PPEELWVALC VSDERRAEWE WVKWLPHNLH PQEQDGAGPA RMVATAFNDL EDLLGAEFTE
     RPVFDPEAVP GRDEPFTVIV VDGVTVPAGH RLDGPGFRNT IVLDLSGSLT WRPGRSTLRL
     DVTPAAVRLV RTDRTRKEQT TLLGRPDRVG PAAAESLARL IAPYRMGLTA DSAEPLAADV
     QLTTLLGIPD LYRHDPTTLW RKHTGAARLR VPVAIGADGG PVELDIKESA QGGMGPHGML
     IGATGSGKSE LLRTLVLGLA LTNSSETLNF ILVDFKGGAT FLGLDELPHT SAVITNLADE
     VALVDRMQDA LHGELIRRQE LLRSAGNYSS ALEYEKARAA GTPLAPLPSL FIVVDEFSEL
     LAAHREFMDL FVMIGRLGRS LGVHLLLASQ RLDEGRMHQL ESHLSYRVGL RTFSAMESRG
     VLGVPDAYQL PSQPGAGFLK SGVDALTRFR AAYVSGPYRH RRGAVVQARV ASQVVPWSAG
     WVVPRTPAAV PEPEREEETE STDSLLSVAL DRLRGHGPTA HQVWLPPLGA PPTLDTLLPG
     LAPTPDRGLS AAGWPGTGRL RVPVGLVDKP FDQRRDPLVV DLSAGGGHVA IAGGSQSGKS
     TVLRTLITSL ALTHTPAEVQ FYCLDFGGGT LSSLAGLPHV GGVAARLDSE RISRTVAEVT
     AVLNQREQFF LDNGIDSMAT YRRRRAAGEF ADETHGDVFL VVDGWAQVKQ NFDSLLPTFN
     QLATGGLNYG IHLIVTTTRW VELSAQIRDQ SATRLELRLG DTMDSVVDVR KAATVPRTPG
     RGLTVGDKLH FLTALPRIDG QNGAEDLADG VTALVEKIAA EWSGPPAPPV RMLPHRLPAS
     ALPPAELGDG LRLPLGLDEE TLSPVWHDFS RTPHLVAIGD AESGKTNLLR LAANAITSRY
     TAAEARVLVV DYRRDLVDAV PAEYQLGHAV SVDALKELVG GSARALKTRL PGPDITPARM
     RLADWWNGPR LFVLVDDYDM VVGSNNFDHP FAPLFDHLAL GHELGLHVIA VRSATGAGRG
     LNDQLLRRLD EVNTPGVLLS CPPSEGYVFG NIKPRNLPPG RAQYVVRRKP TLIQTAEVDN
     ATPPGT
//