ID   D7CAD5_STRBB            Unreviewed;      1318 AA.
AC   D7CAD5;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=ATP/GTP binding protein membrane protein {ECO:0000313|EMBL:ADI06492.1};
GN   OrderedLocusNames=SBI_03371 {ECO:0000313|EMBL:ADI06492.1};
OS   Streptomyces bingchenggensis (strain BCW-1).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=749414 {ECO:0000313|EMBL:ADI06492.1, ECO:0000313|Proteomes:UP000000377};
RN   [1] {ECO:0000313|EMBL:ADI06492.1, ECO:0000313|Proteomes:UP000000377}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCW-1 {ECO:0000313|EMBL:ADI06492.1,
RC   ECO:0000313|Proteomes:UP000000377};
RX   PubMed=20581206; DOI=10.1128/JB.00596-10;
RA   Wang X.J., Yan Y.J., Zhang B., An J., Wang J.J., Tian J., Jiang L.,
RA   Chen Y.H., Huang S.X., Yin M., Zhang J., Gao A.L., Liu C.X., Zhu Z.X.,
RA   Xiang W.S.;
RT   "Genome sequence of the milbemycin-producing bacterium Streptomyces
RT   bingchenggensis.";
RL   J. Bacteriol. 192:4526-4527(2010).
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DR   EMBL; CP002047; ADI06492.1; -; Genomic_DNA.
DR   RefSeq; WP_014175969.1; NC_016582.1.
DR   STRING; 749414.SBI_03371; -.
DR   KEGG; sbh:SBI_03371; -.
DR   PATRIC; fig|749414.3.peg.3492; -.
DR   eggNOG; COG1674; Bacteria.
DR   HOGENOM; CLU_003134_1_0_11; -.
DR   Proteomes; UP000000377; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000000377};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        38..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          449..649
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          812..1004
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   DOMAIN          1100..1283
FT                   /note="FtsK"
FT                   /evidence="ECO:0000259|PROSITE:PS50901"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         472..479
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         831..838
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
FT   BINDING         1117..1124
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00289"
SQ   SEQUENCE   1318 AA;  143706 MW;  6AD6D65A373F1540 CRC64;
     MSQVVVKRQP RALPPEVPSE ELRLESPPEL PRGQQEGVLM QLLPTLGMAS SMVYFFMPGA
     APMMKIMGVM MMFSTLGMTV AMFIRHRQGS QGQLADMRRD YLKYLAQTRR TVRRTARSQR
     DAQFYLHPSP DQLWSVVAEG SRVWERRASD NDFAQIRIGL GSQQLSTPLV APDTAAVDDL
     EPLTAGAMQK FLATQGSLEY MPMAVSLRAF YHVTVSGEPD SVRGTARALV GELATFHSPE
     DLVIAVVAPR SSAAYWDWTK WLPHLQVPGA IDGAGSRRLF SDSLAELEEL LKGRLEGRSR
     FSKDAQPLLD QPHVVVVLDG GMVPPESAFA AQEGLQGVTV IEVVAGDLDE LRGGLSVIVR
     PGKLELLSQV AAYDGAPDSL SLEAADALAR QLAPLRMGGG DDDEPLLANL DFTDLLGLGD
     AGSVDVSRTW RPRSMAERLR VPIGVGEDGS PVMLDLKEAA QDGMGPHGLC VGATGSGKSE
     LLRTLVLGLA VTHSSETLNF VLADFKGGAT FAGMSQLPHV AAVITNLADD LTLVDRMRDS
     ITGELQRRQE LLRSAGNYAN IHDYEKARAA GAPLEPVASL VLVIDEFSEL LTAKPDFIDM
     FIQIGRIGRS LGVHLLLASQ RLEEGRLRGL ETYLSYRIGL RTFSAAESRT ALGVPDAYHL
     PSVPGSGYLK FGTDEMTRFK AAYVSGVYRT GVAPADFDGT SLPIERRPVI FTATPVPVTY
     TTPDPAALTT PSRQEDDALA DTVLDVIVRR LEGQGAPAHQ VWLPPLDEAP SLDQLLPALS
     PVEGRGLTAP EYPRLGNLVV PLGLIDKPFE QRRDVLYRDF SGAAGHMLVV GGPQSGKSTL
     MRTLISAFAL THTPAEVQFY GLDFGGGGMS SVADLPHVGG IASRLDPERV RRTIAEVAGI
     LARREEYFRA KNIDSIGTYR RQRARGEHAE QGWGDVFLII DGWANFRQEY DMLEGVVADI
     AGRGLGYGIH IVVTASRNME VRAALKDQLL NRLEMRLGDT MDSEFDRKVA ANVPVGVPGR
     GQLPEKLHFM GAQPRIDSGS DPEDITDASG ELVRAVTTNW NGPHAPRVRL LPRRLRAEDL
     PKGFEYPQQG IAIGIDETNL EPVFVDFESD PFFLIFGESE SGKTALLRLI AKQITERYGP
     DEAKIVVGDY RRSLLDVIPD SHLLEYAPIA SALQVHTSAL NGLMERRAPK PDITPQQLRD
     RSWWSGPQFF IIIDDYELVS TSSGNPMAVL TDNLPFARDV GMRFIIARNS AGASRSMFES
     FMQRIKELGA QGVMLSGDPT EGDLLGGVRP RPMPPGRGFF VSRKRGTPLV QLGWLPDQ
//