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Entry: A0A010ZQ03_9ACTN
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ID   A0A010ZQ03_9ACTN        Unreviewed;      1317 AA.
AC   A0A010ZQ03;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   08-NOV-2023, entry version 41.
DE   SubName: Full=Type VII secretion protein EccCa/type VII secretion protein EccCb {ECO:0000313|EMBL:EXG79262.1};
GN   ORFNames=CryarDRAFT_0293 {ECO:0000313|EMBL:EXG79262.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG79262.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG79262.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG79262.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases.
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:EXG79262.1}.
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DR   EMBL; JFBT01000001; EXG79262.1; -; Genomic_DNA.
DR   RefSeq; WP_035847793.1; NZ_KK073874.1.
DR   PATRIC; fig|927661.3.peg.280; -.
DR   HOGENOM; CLU_003134_1_0_11; -.
DR   OrthoDB; 9807790at2; -.
DR   Proteomes; UP000021053; Unassembled WGS sequence.
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:SF1; ESX SECRETION SYSTEM PROTEIN YUKB; 1.
DR   PANTHER; PTHR22683; SPORULATION PROTEIN RELATED; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000021053}.
FT   DOMAIN          458..658
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          817..1008
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1098..1282
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          701..741
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         481..488
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         835..842
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1115..1122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1317 AA;  143282 MW;  0AC5375D229A59AC CRC64;
     MGTVIVKRPP RRPAPGFPEG ELILDAPPAI PPPSGRAWGQ AMMMLPMLAG SAAMALMFAG
     TGGAGSTLRW VTGGLFGLSA IGMLSTQLGS YSGQPNKQQM ASQRREYMRH LAQLRRRTRT
     AVQTQREAMF YRHPEPATLW TTAASYRLWE RRPADDDFAV VRIGLGPQDL ATPMVPPAIT
     ASDDLEPLCA QALRRFVTTY AVVPDMPVAL ALNGFARIYL RGDSAHVHGL ARALLAQVTT
     FHAPDDVRVV ICAAPDRLVR WEWVKWLPHA QHPERTDALG PVRLVAPTVM AAEAMLDDLL
     SGRPRFNPTG AGQEVAPHLV VLLDGADPAG SDHLATDNGI EGVTLIDLAA PPLRLLDATV
     LVLDVDRTGR LRSTTMEGDA DIGSADELGT AQAESLARQL APLRLSAAAR GERPLTAEME
     LAELLGLGEP RQFDPANAWR PRPSRERLRV PIGVGQNGAV VELDLKESAQ DGMGPHGLLI
     GATGSGKSEL LRTLVLALAT THSSELLNFV LVDFKGGATF TKLDRLPHTS AVITNLEDEL
     PLVDRMTDAI NGEIRRRQEV LRAAGKFESV RDYEKARAAG APLDPLPSLL IICDEFSELL
     SAKPDFIDMF VQIGRLGRSL GVHLLLASQR LEEGRLRGLD GHLSYRIGLR TFSSMESRVV
     LGVPDAYELP RAPGHGYLKF GTEEMTRFRG AYVSGVYREG GRRAKTSSAE STPVRPFSTA
     YQPLRGELKD ESEPPVPDPD EGVGESLLDI LVERLQGRGV PAHRVWLPPL DQPATLDQLL
     PPLAVEPGRG LTVTDPSRRG ALRAVVGLVD RPLEQRRDLL TLDFSGSQGH AVVVGGPQSG
     KSTLLRSIVA ALALGQTPRE AQFYCLDFGG GALAALRDLP HVGGVASRLE QGKVRRTIAE
     LRTLLLDRER RFAREGIDGM STYRRRREQG EYGDDPFGDV FLVVDNWLTL RNDFEELESQ
     VTDLANRGLS YGIHVLISAS RWMDVRPALR DVLGTRLELR LGEPSDSYLD RRTALNVPDS
     TPGRGITADK FHFLGVLPRV DSRSETADLS DGVAKLVQDM ANAWSGPTAP PVRLLPAEVP
     YASLVGPETL IGIAESDLGP VSVDFTADPH FLLFGDSESG KTAFLRQLAR RITDAHAPDE
     ARLIVVDYRR TLLNEVSPGH LIGYGSSAPV TEQIVDEVAT VMRNRLPGPD VTPEQLRERT
     WWRGPDLYFL VDDYDLVSSG STNPLGPLFE LLAQARDVGL HLIVARRSGG AGRALYDSLL
     LRLRELGSPG LVMSGDRDEG VLLGNVRPQA LPPGRAWFVT RKEGSRLIQL GWLPPSS
//
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