ID A0A0P0SJD1_9PSEU Unreviewed; 1296 AA.
AC A0A0P0SJD1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Secretion protein EccC {ECO:0000313|EMBL:ALL84742.1};
GN ORFNames=AD017_17430 {ECO:0000313|EMBL:ALL84742.1};
OS Pseudonocardia sp. EC080619-01.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1096856 {ECO:0000313|EMBL:ALL84742.1, ECO:0000313|Proteomes:UP000066228};
RN [1] {ECO:0000313|EMBL:ALL84742.1, ECO:0000313|Proteomes:UP000066228}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EC080619-01 {ECO:0000313|EMBL:ALL84742.1,
RC ECO:0000313|Proteomes:UP000066228};
RX PubMed=26535611; DOI=10.1021/jacs.5b09794;
RA Van Arnam E.B., Sit C.S.;
RT "A Rebeccamycin Analog Provides Plasmid-Encoded Niche Defense.";
RL J. Am. Chem. Soc. 137:14272-14274(2015).
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DR EMBL; CP012184; ALL84742.1; -; Genomic_DNA.
DR RefSeq; WP_060574844.1; NZ_CP012184.1.
DR STRING; 1096856.AD017_17430; -.
DR KEGG; pecq:AD017_17430; -.
DR PATRIC; fig|1096856.3.peg.3655; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000066228; Chromosome.
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:UP000066228};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 38..57
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 446..651
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 802..993
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1075..1261
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 985..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 985..1002
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 820..827
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1091..1098
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1296 AA; 135987 MW; 7F97839E4EC13AF5 CRC64;
MAGTVGLRRP RRSVPELPGG ELVLEPPPEP ERPVPGGVAQ RLLPLVMIAG ALLFVVLNPR
ESGSWLFGGM FVLSAAGMLV SGGGRGAGAR TATMDEDRRD YLRYLDVLGA RVRGIAAEQR
CALETVHPEP GAWPDVLAAG RLWERRPGDD DFGRLRAGRG TQRLATRLTA PHTGPLETLE
PLSALALRRF LRRHSTVPGL PVAVDVRVAA TVWLEPLDDA GPATPALDLA RALVAQFVLW
HGPDDARLAV VAPGAAAARW DWAKWLPHVE HPRHHDAVGP VRMITDDPDR VRRWWVDEPS
SAQQHLLVVL DGAADTPGAW AGLPGVTVLR LGPAGRRRPA PSVLRLAAGT GPDGTRTLRR
GGPDGTTVGR PDGVTVAEAR ALARRLARYR PAGAPGTVAG PGTDGPVAGL PSLPGPDVDA
AAVAALRRRR GPAERLRVPI GTDDAGRPVL LDVKESAQGG AGPHGLCIGA TGSGKSELLR
TLVLGLVAAH PADELNLVLV DFKGGATFLG LAGLPHVSAV ITNLAEELAL VDRMADALAG
EITRRQELLR AAGNLASQAE HTAAREAAAR RGEPVPEPLP SLLVVVDEFS ELLAQRPEMI
DLMVTVGRLG RSLGIHLLLA SQRLEEGRLR GLESHLSYRI ALRTFSAAES RAVLGVPDAH
LLPPTPGAAY LSAGTDELVR FRAAYVSAPG PDLPARRHGP AARRVLPFLA GRVSPPAAPD
RPRPAPPVDR FPTVLERVVA AVSGPGPRAH RVWLPPLDEP PPLSTVLGEP AVRSGRGLQA
PGPTGRLVAP IGLVDRPYLQ RRDPLVVDLS GAAGHLAVVG GPRSGKSTAL RTLVVALALT
HTRYELGVHV LDLGGGTLGP LGGLPHVGTV ADRRRTDLVR RVVAEVVATV EHRERLFGTH
GIAGVEDFRT RRAAGELTDE SCTDLLLVVD GYPALRSAGD DLDERLTALA ARGLAYGVHV
AVSAGRWADF RPVLKDQLGS RLELRLGDPS DSETDRRRAA AVPSRPGHGL APDGAAAVVA
APVTVTGADP APPVAAAWPG AGLPAVRLLP ERITVEELPP GPGRGPALGV DEDRLSTVEL
DPDEPHLLCF ADSGGGKTNL LRLIARGIAA RRTPEEARIV VVDHRRTLLG AVPPSHLLAH
AATAGATAEA CADVAGSLGR RLPGAGVTPA QLRERSWWSG PDVWVLVDDY DLVVPAAGSS
GGHPLLPLAE YLPQARDVGL HVVVARRTGG ASRALFDPVL GRLRELGAPG LVGAGSPDEG
ALLEKVKPGP MPPGRAVLVD RGHGARRVQL AWTEPE
//
