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Database: UniProt
Entry: A0A223SD31_9ACTN
LinkDB: A0A223SD31_9ACTN
Original site: A0A223SD31_9ACTN 
ID   A0A223SD31_9ACTN        Unreviewed;      1319 AA.
AC   A0A223SD31;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Type VII secretion protein EccC {ECO:0000313|EMBL:ASU86012.1};
GN   ORFNames=CDO52_03665 {ECO:0000313|EMBL:ASU86012.1};
OS   Nocardiopsis gilva YIM 90087.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1235441 {ECO:0000313|EMBL:ASU86012.1, ECO:0000313|Proteomes:UP000215005};
RN   [1] {ECO:0000313|EMBL:ASU86012.1, ECO:0000313|Proteomes:UP000215005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90087 {ECO:0000313|EMBL:ASU86012.1,
RC   ECO:0000313|Proteomes:UP000215005};
RA   Yin M., Tang S.;
RT   "The complete genome sequence of Nocardiopsis gilva YIM 90087.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP022753; ASU86012.1; -; Genomic_DNA.
DR   KEGG; ngv:CDO52_03665; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000215005; 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:SF1; ESX SECRETION SYSTEM PROTEIN YUKB; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 1.
DR   Pfam; PF01580; FtsK_SpoIIIE; 3.
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:UP000215005};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        36..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          456..656
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          816..1007
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1101..1283
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          348..380
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1286..1319
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         479..486
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         834..841
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1118..1125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1319 AA;  141869 MW;  06B29D29D23AD0B7 CRC64;
     MPDNPPASSS MSMMLMPVIS GSGSLLMAVT MGNRPLYAAG AMLVMLASIA VGVTMFLSQR
     NGPRKRIREQ RERYLDYLDQ LRDTVRDVAA TQRKGSAFRH PAPHLLAEPA RLPARRWERR
     ASDPDFLHLR VGTGTRPLAR PLSLKVDASN PLVVYDPVCQ GLADQLVELY AHVPEEPLVM
     PLRELGVVSV IGDRAAGRAL ARSLVAQLAT FSAPEDVRVG VVRHARLLPE WDWLKWLPHN
     AHDDITDGPL PARLVAGNTV EMAELLSAEI EQRTIDMQRR RGRPPGPGTQ RLVMIVDGEF
     QATLSGLSAE PPVASLADLG IHLIMLLGER REEPEQVDMR LYVTADGELT EDTDDSAQGA
     NSAGGSGAMG HEPEAPRAPL KGTADQASVA LLTSLSRTLS PMRLAATDGA DALHSTVDLP
     EILGVPDVAQ LDARQTWRPR STSDYLRVPI GIGPSGNLVL LDLKESAFGG MGPHGLVVGA
     TGSGKSEMLR TLVASLVINH APDHLALLLV DFKGGATFAD TDRLPHSAGL ITNLADDDTL
     VARFREAMYG ELTRRQQLLK DAGNLPNLHA YEALRAQQPD LEPLPHLLVI IDEFSELLTA
     HPDFAELFVA IGRIGRSIGV HLLLATQRLE SGKIKGLESH LSYRIGLRTF SESESREAIG
     VGDAYHLPPE PGSGYLKVDT SVFERFKAAM VSGPYIPPAE ATNDDDPVLP VISYNGVGAL
     LGLSDLVGED ADESGGDGSS SRSVLQVAVD RLVAAGAEPV RPVWLPPLPT ALTLDTLFEQ
     VATEDGSAAD KEEAEPDAAE MCAYIGLTDI PRDQRQEPTA VDFTGGDSNI VVLGGPQTGK
     STLLRTMIAS LAWRYPPGRV AIYAVDFGGG GLAALEGLPH VAGVAGRADP ERVQRILSDV
     STQLDQREQV FRSVGLDSPA GLRKARAEGK VPEGIAGDVF LMIDGWSSVR ENFEDADDVL
     LDIVTRGPSL GVHTILTGAA SSQVRSKLAA FFGGRIELRL TDPFDSGIGR KVAEEIPKDV
     PGRALLADEN MAHIALPRVD GVADDQDLGE GVRDLVAQVS KRWTARAVQQ VRTLPDLVEL
     DELTRTHDGP ELVLGMAERT LEPALLQLSE EPHLMVFGDP QTGKSTLLRG LLRQLTQRPP
     EEVGIVLVDF KRAHLGVVGE EHLLAYCTEA QFTQQIAGQL AGSVKERLPG PDVTPQQLRE
     RSWWKGLELF VVVDDLDLIS NRQGNPLAPL AQFIPQGADL GLHLIAARRT GGAGRALFEP
     IPQALTDAAT TGVLFSGDRM EGRLANGVAS RPLPPGRALL ARRGQRPEQL QAPWSDPPE
//
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