ID A0A124H8N7_9ACTN Unreviewed; 1312 AA.
AC A0A124H8N7;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Secretion protein EccC {ECO:0000313|EMBL:KUM82698.1};
GN ORFNames=AQI94_38680 {ECO:0000313|EMBL:KUM82698.1};
OS Streptomyces pseudovenezuelae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=67350 {ECO:0000313|EMBL:KUM82698.1, ECO:0000313|Proteomes:UP000053039};
RN [1] {ECO:0000313|EMBL:KUM82698.1, ECO:0000313|Proteomes:UP000053039}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40212 {ECO:0000313|EMBL:KUM82698.1,
RC ECO:0000313|Proteomes:UP000053039};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces pseudovenezuelae DSM 40212, type
RT strain for the species Streptomyces pseudovenezuelae.";
RL Submitted (OCT-2015) 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:KUM82698.1}.
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DR EMBL; LMWM01000050; KUM82698.1; -; Genomic_DNA.
DR RefSeq; WP_031038040.1; NZ_KQ948154.1.
DR OrthoDB; 9807790at2; -.
DR Proteomes; UP000053039; 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}; 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..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 448..648
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 806..998
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1094..1277
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT REGION 1278..1312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1280..1312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 471..478
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 825..832
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1111..1118
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1312 AA; 142879 MW; DA858352A7A91867 CRC64;
MSVVIVKRPP RVFPPEVPSE EVKLESPPEL PRTEDDSLLM NLLPMLGMGS SAAFFFMPGA
QGFMKIMGGL MMVSTVAMLV AQIVRARKGP SGQMAEARRD YLKYLAQKRR EVRRTVHKQR
DAQYYLHPAP EQLWALVAEG SRLWERRSMD PDFVQVRIGL GPQQLATPLV APDTAPVDEL
EPLTAHAMQQ FIASYGTLGE LPLAIGLRSF YHVTISGDAE TVYGQTRSVV GQLASLHSPE
DVVIAVVASP GAAVDWEWTK WLPHMQHKES DGAGTRRLLC YDLGELEEMI AHQLEGRPRW
SRDGSPVLDQ PHVVVVLDGG GVPADSVLAS AEGLQGVTIL EVVPGELDEA RGSLSVRVWP
DAMELEAGTG VFTGVPDVLS QAQAESLGRQ LAPLRLGAAD ADEPLLANLD FTDLMQIGDA
ASVDVSRTWR PRTLHERLRV PIGLGESGEP VMLDLKEASQ EGMGPHGLCV GATGSGKSEL
LRTLVLGLAV THSSETLNFV LADFKGGATF TGMGSMPHVS AVITNLADEL TLVDRMRDSI
TGELTRRQEL LRTAGNYANI TDYEKARAAG AALDPLPSLV LIIDEFSELL AAKPDFIEMF
IQIGRIGRSL GVHMLLASQR LEEGKLRGLD TFLSYRIGLR TFSAAESRTA IGVPDAYHLP
NVPGAGILKY DTETMVQFKA AYVSGTYRPN GPMAQGGGRI DRSPVLFTAS PVPVRILTEP
EPETRTHQVD DALADTVLDV IVSRLDGQGP PAHQVWLPPL DEPFSLDQVL PALGISPERG
LHAEGYHLQS KLTVPVGLVD KPFEQRRDVM YADLSGSAGH ALIVGGPQSG KSTLVRTMIT
SFALTHTPAE VQFYALDFGG GGMLALENLA HVGGAASRLD QEKVRRTVAE VHGILNAREE
FFRSKSIDSM GTFRNRRAQG HYPDQQWGDV FLIIDGWATF KNDYEMLDPV IADIATRGLG
FGVHLIITAT RYTEMRPALR DQILSRLELR LGDAMESEFD RKRAENVPMG KPGRGLSPDK
LDYLAATPRI DGSTAVEDLA DGMAHLVQSV NNAWQGPTAP KVRMLPTMLH ASELPGGGDF
GNRGIAVGVD ELTLSPVFVD FETDPLFVIY GESESGKSSL LRFMAKQISE RYAPNKALFV
VSDFRRALLG QVPESHMYKY CASGPQLQEV MESLAGSMSR RMPGPDVTPD QLRNRSWYNE
PDAFIFIDDY DLVATSMGNP MSVLLEYLPF ARDLGLRIIL ARSTSGASRS SFEPVLTRIK
ELGAQGIVLS GDPSEGPVFN NIKATPQPQG RGQFISRRSS GQLVQTGYLP ES
//