ID A0A229T6V3_9PSEU Unreviewed; 1338 AA.
AC A0A229T6V3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Type VII secretion protein EccC {ECO:0000313|EMBL:OXM66975.1};
GN ORFNames=CF165_19635 {ECO:0000313|EMBL:OXM66975.1};
OS Amycolatopsis vastitatis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=1905142 {ECO:0000313|EMBL:OXM66975.1, ECO:0000313|Proteomes:UP000215199};
RN [1] {ECO:0000313|Proteomes:UP000215199}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H5 {ECO:0000313|Proteomes:UP000215199};
RA Adamek M., Alanjary M., Sales-Ortells H., Goodfellow M., Bull A.T.,
RA Kalinowski J., Ziemert N.;
RT "Comparative genome mining reveals phylogenetic distribution patterns of
RT secondary metabolites in Amycolatopsis.";
RL Submitted (JUL-2017) 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:OXM66975.1}.
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DR EMBL; NMUL01000016; OXM66975.1; -; Genomic_DNA.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000215199; 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; 2.
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 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 461..661
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 829..1023
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1120..1304
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 735..757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 484..491
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 847..854
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1137..1144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1338 AA; 146821 MW; 5A8791A46449F44B CRC64;
MSTLQFKKSP RLAAPRPPGG EVHLEPPPEV PRVIPGNVVM KALPVVMIVA SLGMMVFMFQ
ASNRNPMMMA MGGMMVVGTL GMMAGGGGGK GGGAKRAEMD EDRKDYLRYL GQMRDRAREA
MVDQRAALEW VHPDPQSLWS LAASRRMWER RQNDQDFLHL RVGRSSHRLA TRLVPPQTGP
VDELEPIATL ALRRFVRAHS IVPDLPTQIT LRGFAAVSMQ GDRALTRGLT RAMLAQLVSF
HSPDDVLIAV ATAGRAKEEW EWAKWLPHAQ HPTLADGIGQ LRMMAGSLAQ IENWLDEELR
DRQRFSRNAT PAPDQPHVVI IIDDAEVTRE EQIVLEEGLV GVTLIDLSDS LGNLAARRGL
RLVVEPDRLG ARSAGGVEWF GRPDTLSLVE TESLARLISP YRVGGAAGQD VGDEEPLLSN
PSLLELLGIP GDPMTFDVQQ AWRPRPIRDR YRVPFGVGEY GQPVELDIKE AAAEGMGPHG
LCIGATGSGK SEFLRTLVLG LLSTHSSSTL NFVLVDFKGG ATFMGLDKAP HVSAVITNLA
DEVTLVDRMK DALAGEMNRR QEALKNGGNF KNVWEYEKAR ENGADLDPLP ALFIVCDEFS
ELLSAKPDFI DLFVAIGRLG RSLQMHMLLA SQRLEEGKLR GLDSHLSYRI GLKTFSAAES
RAAIGVPDAF ELPSVPGGGY LKYDTSTLVR FKAAYVSGPY RPAGIKAAGP AATVVRADKR
PQLFVPDFVE LPKEPEPQLI EAPKQEEQRQ PEEAVEPSEL DVIVSRLVGQ GPPAHEVWLP
PLKDPNSLDT LLPNLNPTDD RGLSPVGFFG NGRLQVPLGI IDRPYEQRRD PLWADFSGAA
GHGVIVGGPQ TGKSTMLRTL IMSMALTHTP EEAQFYCLDL GGGTLAGLAD LPHVGGVAVA
RREPDKARRI VAELTTLLTE REGRFGAMGI DSMTEFRNRK RRGEIRPDQD PFGDAFLVVD
NWRALRDDFE ELETTITRLA TQGLSYGVHV IIAANRWADI RPAIKDMLGT RFELRLGDPT
ESDIDRRIAV NIPAGRPGRG LTREKLHMLG GLPRIDGSSD PETVAAGVAD AVAKIRAAWR
GRVAPQVRLL PELITYEEVL KIDSARDSKL IPIGVNEEDL QPIYLDFNAE PHFYAFADGE
SGKTNLLRQI ARGISERYTA QEALILLVDY RRTMLGFVQG DSLLGYAVSA NQLESMINDV
FNSMTRRLPG PDVTQEQLKT RSWWKGPELF VLVDDYDLVA TSTTNPLRKI SDFLAQAKDV
GLHLVVVRRT GGASKAMYDP IIGKLKEIAA PGMVMNGSRD EGMLVGNIKP SAMPPGRGNL
LTRKNGKQLI QVSWIQPD
//
