ID A0A1Q4YUW5_9ACTN Unreviewed; 1335 AA.
AC A0A1Q4YUW5;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Type VII secretion protein EccC {ECO:0000313|EMBL:OKI38367.1};
GN ORFNames=A6A29_10385 {ECO:0000313|EMBL:OKI38367.1};
OS Streptomyces sp. TSRI0281.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718998 {ECO:0000313|EMBL:OKI38367.1, ECO:0000313|Proteomes:UP000186952};
RN [1] {ECO:0000313|EMBL:OKI38367.1, ECO:0000313|Proteomes:UP000186952}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0281 {ECO:0000313|EMBL:OKI38367.1,
RC ECO:0000313|Proteomes:UP000186952};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKI38367.1}.
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DR EMBL; LWLE01000023; OKI38367.1; -; Genomic_DNA.
DR RefSeq; WP_073723442.1; NZ_LWLE01000023.1.
DR STRING; 1718998.A6A29_10385; -.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000186952; 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; 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}; Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00289}; Reference proteome {ECO:0000313|Proteomes:UP000186952};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 466..667
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 831..1022
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1117..1302
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 97..124
FT /evidence="ECO:0000256|SAM:Coils"
FT BINDING 489..496
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 849..856
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1135..1142
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1335 AA; 143723 MW; 62522930791727E1 CRC64;
MSTRLIHRPA RTTRPPATSA PRTIEAPPNL PEGKAGNIAM SLLPVAGVMS SVVMMTVVRN
SQFAALGAII LVVTIIGSVA LLFSQRGKAQ RTRRTQREAY LAYVEDLREE LSSEERERRE
RADVLNPSPY ALYDIVRDPA RLWERRRADD DFLRVRVGTG EMPVRDLRIA EQGSSVLTPP
DLFMLNEASA LTNRFRNGTE LPLTVPLDRV GNISVIGPRA DCLRVARALL VQAAALHAPD
DVALAVAAPG DRIADWEWAK WLPHLLDPER FDGPVAARRI APSAPQLARQ LGAELRRRAS
YAAEVRRGLA GKDALSMNSR LLVVTDGHGE DAVDLPRPDD AVGLREMGVT VLHLLEQRVQ
EPGHVNVRIT VDGPDVTIED LRAGEPIEAR GTVDEVGIPF AEGLARMLAP LRLSAESLVD
APLSGPVEFA SMLGIDDVAQ LDLPALWAPR GERAFLRVPI GISDSHEPVL LDLKESSELG
MGPHGLCVGA TGSGKSELLR TLVLALVATH PPEDLALVLV DYKGGATFAP FADLPHVSGV
ITNLENQAGL VERVHSSLAG EVKRRQQALK DAGNVADIGD YAALRAEKRP DLDPLPHLFV
VIDEFGELLT AKPDFIDLFL SIGRIGRSIG VHLLLSSQRI EGGKLKGLDT YLSYRLGLRT
FSADESRTVL DTTDAFHLPP LPGFGYLKVD TSHYARFKAG YVSGGYRGPV RHSEDEETGP
LALAYEAFNT LAGPDAAQPQ EPASRRRETG PTELGVMVAQ LTGAAPPVRG IWLPPLPAAT
ALDTVAGPLD IGPRGMRLAG ARADGGRAGA RRQGPLLVPL GLLDDPAKQW QGRWFLDLTV
AGGHAAVIGG PQSGKTTLLR TLVLSLALTH TPQEVGVYGL DLVGGGLQAL SDLPHVGGIA
GRADRERAAR TVEEVRTMLA LREDLFREHG IDSVEQLRTL HAAGRLPQLA SAEILLVIDG
FGALRDDFEE MDDAIGDILK RGGGYGIHVV AGMLRWNDVR IAIQSNFGTR MELRLNDSGE
SSIDRKLAGT LSPEEPGRVL TDGKLFAQVA LPRTDGVTDT ADLGAVLERT ARTLRATWNG
DVAQPVRVLP HTLEPHLLPG PAAEPRRVAI GLDQSALAPV LLDLFHHDQH LLVMGDSECG
KTNLLRTVAH GLIDRYGEDD LVFAVMDPRR SLRGAVPEEF NGGYAYNSKL CAGLSAGIAT
ELEKRLPDEN ARLEDLEPGS WGKGPRIVVL VDDYDVLTTA GQSPLAAFLP YIPSAVDIGL
HFVLTRRVAG ASRGMYEPLV QGLRESGASA LLMAGDRSEG QLFPGVYASQ QAPGRGVFIR
RGQPNRLIQT VRSPG
//
