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Database: UniProt
Entry: A0A344L7S5_9PSEU
LinkDB: A0A344L7S5_9PSEU
Original site: A0A344L7S5_9PSEU 
ID   A0A344L7S5_9PSEU        Unreviewed;      1316 AA.
AC   A0A344L7S5;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Type VII secretion protein EccC {ECO:0000313|EMBL:AXB44099.1};
GN   ORFNames=A4R43_17505 {ECO:0000313|EMBL:AXB44099.1};
OS   Amycolatopsis albispora.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=1804986 {ECO:0000313|EMBL:AXB44099.1, ECO:0000313|Proteomes:UP000250434};
RN   [1] {ECO:0000313|EMBL:AXB44099.1, ECO:0000313|Proteomes:UP000250434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP1 {ECO:0000313|EMBL:AXB44099.1,
RC   ECO:0000313|Proteomes:UP000250434};
RA   Wang H., Chen S., Wu Q.;
RT   "Complete genome sequence and analysis of deep-sea sediment isolate,
RT   Amycolatopsis sp. WP1.";
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP015163; AXB44099.1; -; Genomic_DNA.
DR   KEGG; aab:A4R43_17505; -.
DR   Proteomes; UP000250434; 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; 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}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        62..83
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..1004
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1097..1281
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         1114..1121
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1316 AA;  140509 MW;  0B08A46F0351F445 CRC64;
     MTLARDRLPL AGEQPGEIVL QSPPMLPKGG SGGALQLMLF LPMMLGMGAM SFVYIGRDGG
     AMTWVFGALF ITAMGGMIVM SLARGGQQKK AQINEERRDY QRYLAGLRGQ VRDIAGNQRS
     AMISQQPEPA DLWAYVTSGR MWDRRRHDGH FGQVRVGTGP QRLMTPLKAP QTVPLEDLDP
     VSSTSLRHFI RTYSTVDGLP VAISLRSFAT VSVSGRRGEV LDLARAVLAQ LATFHSPNDL
     RIALCAPAER QAEWDWLKWL PHAGSATGTD AAGPARLVAE NLAGLVDALG QDLGERAAFT
     RAAGLGHDLP HIVLVVDGGD TDGDTRLMPH GGKHGITVLD VGAEEPRAVP SDRTLCLHTD
     RTRLGMLVGE GSEQQLGFLG VPDGLDAGAA EALARRLTPL HQVGTVVTGD NPMSSTFGLA
     GLLGIGDPRD VDTSVTWVAR AARDRLRVPL GVDPEGRPVE LDLKESAEGG MGPHGLVIGA
     TGSGKSELLR TLVTALAVTH SSERLNLALI DFKGGATFAG MTHLPHTCAV ITNLSEELIL
     VDRMADAING EVIRRQELLR AAGNYASARD YERAREAGAN LRPLPSLLVI IDEFSELLSA
     RPEFIDLFVS IGRLGRSLGI HLLLASQRLE EGRLRGLDSH LSYRIGLRTF SASESRAVLG
     VADAYQLPPV PGSAYLKADT DSLIRLKAAY VSGELPPRQV VREKGAPAQH IVPFTLGPVS
     PPVPVEPGED EIVYEEPSTG ETVIDAMLSR LDGPAAHQIW LPPLAEPPTL DQLLPPLGET
     PERGLHPVGW GGNGRLTVPV ALVDKPLEQR RDLLWADFSG AGGHALVVGA PQTGKSTLLR
     AVVGVLALTH TPAEAQFFLL DMGGGALSPV AGLPHVSGYA TRRDAQRCRR VVAEVTTLLE
     QREEFFAANG IESAAEFRGR RAEFAESTDG REFGDVFLVV DDWATVRKDY EQLEEQITAL
     AARGLGFGIH VVISANTWMG VRAQLRDAIG TRFELRLGDP GDSLIDRKAA RNVPAEAPGR
     GITADKLHFL GALPRVDGDQ RAATIGVGAT DLVRRISESW QGDPAPQVRL LPARIELSGL
     PPAPPKQVTL GVAESTLEPV LLDFGADPHF LAFGDVESGK TALLRVIGQG IMSAYSDDDA
     AIIVADYRRG LLDAVTGRHL LGYAGSAPTL TGLINEVVQA MRLRLPGPDV TAEQLRNRSW
     WTGPELFVLV DDYELVATAG SNPLLPLLEF LPQARDIGLH LVIARGSGGA GRALFEPVVQ
     RVRELGSPGL VMSGSKDEGP LIGDVKAGPL PPGRGTLVSR RLGTGLLQVA WTPPAD
//
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