ID A0A124HQE8_9ACTN Unreviewed; 1370 AA.
AC A0A124HQE8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Secretion protein EccC {ECO:0000313|EMBL:KUN35158.1};
GN ORFNames=AQJ30_27235 {ECO:0000313|EMBL:KUN35158.1};
OS Streptomyces longwoodensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=68231 {ECO:0000313|EMBL:KUN35158.1, ECO:0000313|Proteomes:UP000053271};
RN [1] {ECO:0000313|EMBL:KUN35158.1, ECO:0000313|Proteomes:UP000053271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41677 {ECO:0000313|EMBL:KUN35158.1,
RC ECO:0000313|Proteomes:UP000053271};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces longwoodensis DSM 41677, type strain
RT for the species Streptomyces longwoodensis.";
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:KUN35158.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMWS01000034; KUN35158.1; -; Genomic_DNA.
DR STRING; 68231.AQJ30_27235; -.
DR Proteomes; UP000053271; 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; 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; SPORULATION PROTEIN RELATED; 1.
DR PANTHER; PTHR22683:SF1; TYPE VII SECRETION SYSTEM PROTEIN ESSC; 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:UP000053271};
KW 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 TRANSMEM 63..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 451..651
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 861..1054
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT DOMAIN 1150..1333
FT /note="FtsK"
FT /evidence="ECO:0000259|PROSITE:PS50901"
FT BINDING 474..481
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 879..886
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT BINDING 1167..1174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ SEQUENCE 1370 AA; 145688 MW; E7911DCED1FC0354 CRC64;
MSHVVVKRPP RTLPKEVPTE EVVLQPPPEL PRGQREGALL QLLPMLGMGG SVVFFFNPQA
QPFMKIMGMV MVASTLALGV SMLVRYRRGN IGQLADLRRD YLRYLSQVRR AAQDTARAQR
DAQFYLHPSP EQLWALVAEG SRVWERRSGD EDFGQVRVGL GVQPLSTPLV PPQSAPTDQL
EPMTAGAVER FVATHGLLED LPIALSLRAF FHLTISGDPA TVRGATRAVT ASLTALHSPA
DLVVAVAAAP ESAPEWEWVK WLPHAQAPGL ADGAGSVRLI SADPLELEDL LGARLQGRPR
FHPAGPPVPE QPHVVVVLDG VSLPPTSLLA SPEGLQGVTL LEVVPGELAH GRGDLSVVVR
PTSLLLESAQ GPAYEGTPDV LSYEAAEALA RQLAPLRVAS GGDDDEPLLA RLEFTDLLDL
GDAAAVDPRH TWRPRGQAER LRVPIGVGED GRPVLLDLKE AAHEGMGPHG LCVGATGSGK
SELLRTLVLG LAVTHSSETL NFVLADFKGG ATFAGMAHLP HVAAVITNLA DDLTLVDRMG
DSLRGELNRR QEMLHGAGNY ANIHAYEKAR AAGAPLQPMP SLVLVIDEFS ELLTAKPDFI
EVFVQIGRIG RSLGVHLLLA SQRLEEGRLR GLETHLSYRI GLRTFSAAES RAALGVPDAY
ELPNVPGSGL LKFGTDELVR FKAAYVSGAY RSGAPRVSSG GLLPADRRPV LFTAARVPVG
RGVLPHQRGA SGDGAGVAGG AGPGAGAGAA GVAGVGSGAD VGGGAGGGSG ASGGTGTGAG
SIDDDALADT VLDVVVRRLE AQGPAAHQVW LPPLDSPPSL DALLPGLAPV AGRGLTLPGY
EGAGRFVVPV GIVDKPYEQR RDPLWADFGG SAGHMQILGG PQSGKSTLVR TVVASFALTH
TPHEVQFYAL DFGGGGLSAV AGLPHVGGVA SRLDPERVRR TTAEVYGIMN RREEYFRSAG
ISSVADFRAR RARGDIPLTD QPWGDVFLVI DGWGAFRTEY EALEPVVLDI AARGLGFGIH
LVLTASRAME VRANLKDHLM NRLELRLGDA MDSEFDRKVA ANVPTGVPGR GQTPQRQHFM
AAVPRIDGLS SDADLPDATS ALVAEVGRHW QQPGAPGVRL LPRSFAADRL PSGDRFPERG
VSFALDEDHL EPVFVDFDQD PFFLVLGESE SGKSNLLRLL VRRLGERYDG DHCKLFVVDN
RRSLLGVTPP SHLAEYIPVS NQMQHHMDAL ADLMRRRTPT ADVTPEQLRE RSWWRGPTVF
VVIDDYDLVA TSSGNPLAGL TELLPFARDV GVRFIIARST AGAGRASYEP FMQRMKELGA
QGVVLAGDPA EGDLLGGVRP RAMPAGRGIF VSRRRGKPMV QVGLAGEVGE
//