ID A0A1E7K819_9ACTN Unreviewed; 1324 AA.
AC A0A1E7K819;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Secretion protein EccC {ECO:0000313|EMBL:OEV00075.1};
GN ORFNames=AN217_22210 {ECO:0000313|EMBL:OEV00075.1};
OS Streptomyces qinglanensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=943816 {ECO:0000313|EMBL:OEV00075.1, ECO:0000313|Proteomes:UP000175829};
RN [1] {ECO:0000313|EMBL:OEV00075.1, ECO:0000313|Proteomes:UP000175829}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO M10379 {ECO:0000313|EMBL:OEV00075.1,
RC ECO:0000313|Proteomes:UP000175829};
RX PubMed=27446038; DOI=10.3389/fmicb.2016.00998;
RA Tian X., Zhang Z., Yang T., Chen M., Li J., Chen F., Yang J., Li W.,
RA Zhang B., Zhang Z., Wu J., Zhang C., Long L., Xiao J.;
RT "Comparative Genomics Analysis of Streptomyces Species Reveals Their
RT Adaptation to the Marine Environment and Their Diversity at the Genomic
RT Level.";
RL Front. Microbiol. 7:998-998(2016).
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:OEV00075.1}.
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DR EMBL; LJGV01000022; OEV00075.1; -; Genomic_DNA.
DR RefSeq; WP_069992678.1; NZ_LJGV01000022.1.
DR PATRIC; fig|943816.4.peg.3988; -.
DR Proteomes; UP000175829; 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; 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:UP000175829};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 453..653
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 818..1009
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1105..1288
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 476..483
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 836..843
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1122..1129
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1324 AA; 143606 MW; C7E8E2C4B9016CEC CRC64;
MTQIVVKRPP RALPPDVAAE ELQLQPPPEL PKNKQEGMWM QLLPMLGMGG SSVYFLMPGM
NSHPMMKIMG VLMLFSTLTM VIAMVVRMRR GTQGEMAQTR RDYLKYLAQT RRTVRRTAVK
QRDAQFYLHP APEQLWSLVA EGSRVWERRP SDLDFGQVRV GLGVQQLATP LVSPDTAPVD
ELEPLTAGAM HQFINTHATL DGLPMAISLR AFYHMTVSGD PDAVYASARA LLCSLCAMHS
PEDLVVAVAA GRESYAGWDW AKWLPHAQAR GETDGAGSRR LIVGDTLELE ELLAARLEGR
PRFNGTAEPA PDQPHLVVVL DGTSLLPNSL LSAPEGLQGV TIVEVVPGDI DVARGTLSVV
VGPRSLRLES GHGLVYEGTP DALSYPAAEA VARQLAPLRV GSGDDGDEPL LAKLEFTDLL
NLGDAASVDV SRTWRPRSQA ERLRVPIGVG EDGQPVMLDL KEAAQDGMGP HGLCVGATGS
GKSELLRTLV LGLAVTHSSE TLNFVLADFK GGATFAGMAH MPHVAAVITN LADDLTLVDR
MGDSIRGELN RRQEMLRDAG NYANIHDYEK ARAAGAPLSA IPSLVLVIDE FSELLTAKPD
FIDMFIQIGR IGRSLGVHLL LASQRLEEGR LRGLETYLSY RIGLRTFSSA ESRAALGVPD
AYHLPSVPGS GYLKFGTDEM TRFKAAYVSG VHRTGGDELP AGPLAPNRRP VLFTAAEVAV
QHPDPDTVPV PTQPAPAAAD DDALADTVLD VVVRRLEGQG TPAHQVWLPP LDNASPLDEL
LPSLAPVEGR GLAATDYQRQ GRLVVPVGLV DKPFEQRRDP LYLDFSGAAG HMLVVGGPQS
GKSTLMRTLV SSFALTHTPA EVQFYGLDFG GGGMSAVSGL PHVGGIASRL DPERVRRTVA
EVYGILNRRE EYFRANSIDS ISTYRRRRAR GQITDQPWGD VFLVIDGWGN FRNDYEGLTE
VVSDIAGRGL GYGVHLVITA SRNMEVRAAL KDLLMNRLEL RLGDTMDSEF NRKVAANVPP
GVPGRGQTMD ALHFMAGVPR IDGVGSDEEL ADASAEMCTA VASQWPGEPA PQVRLLPREL
PAGRLPGGAE HPERGVAFAI DENNLEPVFV DFDTDPFFLV FGESESGKTA LLRLLVKQIS
ERYSGDEAKI VVGDYRRALL GTIPDSHLLE YAPMSNTMET HMNALRDLMD RRAPSSDVTP
QQLRDRSWWT GPQIFIVVDD YELVATSSGN PLAVLTEHLP FSRDVGVRFI IARSAAGASR
SMFESFMTRI KELGAQGVLL SGDPSEGDLL GNVRPRPMPP GRGFFVSRKR GTPLVQLGWL
PDET
//
