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Database: UniProt
Entry: A0A2T7SPD1_9ACTN
LinkDB: A0A2T7SPD1_9ACTN
Original site: A0A2T7SPD1_9ACTN 
ID   A0A2T7SPD1_9ACTN        Unreviewed;       805 AA.
AC   A0A2T7SPD1;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Sporulation protein {ECO:0000313|EMBL:PVE04860.1};
GN   ORFNames=Y717_09305 {ECO:0000313|EMBL:PVE04860.1};
OS   Streptomyces scopuliridis RB72.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1440053 {ECO:0000313|EMBL:PVE04860.1, ECO:0000313|Proteomes:UP000245992};
RN   [1] {ECO:0000313|EMBL:PVE04860.1, ECO:0000313|Proteomes:UP000245992}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RB72 {ECO:0000313|EMBL:PVE04860.1,
RC   ECO:0000313|Proteomes:UP000245992};
RA   Olson J.B.;
RT   "Annotated genome of Streptomyces scopuliridis.";
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the CbxX/CfxQ family.
CC       {ECO:0000256|ARBA:ARBA00010378}.
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:PVE04860.1}.
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DR   EMBL; AZSP01000378; PVE04860.1; -; Genomic_DNA.
DR   RefSeq; WP_030349611.1; NZ_JOEI01000002.1.
DR   AlphaFoldDB; A0A2T7SPD1; -.
DR   STRING; 1440053.GCA_000718095_00394; -.
DR   OrthoDB; 9806903at2; -.
DR   Proteomes; UP000245992; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041627; AAA_lid_6.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR039448; Beta_helix.
DR   InterPro; IPR006633; Carb-bd_sugar_hydrolysis-dom.
DR   InterPro; IPR000641; CbxX/CfxQ.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   PANTHER; PTHR43392; AAA-TYPE ATPASE FAMILY PROTEIN / ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR   PANTHER; PTHR43392:SF2; AAA-TYPE ATPASE FAMILY PROTEIN _ ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17866; AAA_lid_6; 1.
DR   Pfam; PF13229; Beta_helix; 2.
DR   PRINTS; PR00819; CBXCFQXSUPER.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00722; CASH; 2.
DR   SMART; SM00710; PbH1; 14.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000245992}.
FT   DOMAIN          41..172
FT                   /note="Carbohydrate-binding/sugar hydrolysis"
FT                   /evidence="ECO:0000259|SMART:SM00722"
FT   DOMAIN          313..474
FT                   /note="Carbohydrate-binding/sugar hydrolysis"
FT                   /evidence="ECO:0000259|SMART:SM00722"
FT   DOMAIN          582..722
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   REGION          478..499
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   805 AA;  85187 MW;  67293C7638B11FEA CRC64;
     MAQGTVQVTH TGTSRWRRRT GEYASLAAAL EAAGDGDVLT IAPGTYRENL IVTRAVTLRG
     PEGSLGSVRI APADGVPLTV RASATVQDLH VEGQDSAAPA LLVEDGTPEL SDLRIVTRSA
     AGLEVRGAAR PTVRRCTVDN PAGVGIGVLD GAGGVFEDCE IVAAGQSGIS VRGGAHPRLE
     RCRIHHASGS GLSVTGEGSG LEAVGCEVYE IKGTGVQIAS RAAAHLTDSS VHRTSADGIT
     LDTDAVLTLS DCDIHDIPEN AVDLRSRSVL TLTRSTVRRF GRNGLSVWDP GTRVDANQCE
     IHDSTGDYPA VWVSDGATVV LDSCRVHDVP DALFVLDRGS RADVVDTDIS QVRNTAVSVS
     DGATAQLDDC RIREASTGAW FRDHGSGGTL NSCTIDGVQT GVIVTKGADP TIERCTVTSP
     AEAGFYVSAE GRGTFHSCRV TGSGGYGFHV MDGCRTTLTR CRTERCARGG YDFAEDGPTV
     EDCTSDESGV LTPPTPSLEP SAVLTATQST GLLGAVPAQS ATARPSDAIP EATKPARASE
     AVLGELDSLV GLDSVKREVR ALTDMIEVGR RRKEAGLKAA SVRRHLVFTG SPGTGKTTVA
     RLYGEILHSL GVLERGHLVE VSRVDLVGEH IGSTAIRTQE AFDRARGGVL FIDEAYALSP
     EDSGRDFGKE AIDTLVKLME DHREAVVVIV AGYTAEMERF LTVNPGVASR FSRTITFSDY
     VPEELLRIVE QQSEEQEYRL GEGTAEALLK YFTVLPKGPA FGNGRTARQT FESMVERHAG
     RVAQLPETST DDLTLLYADD LPELP
//
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