ID D9VN94_9ACTN Unreviewed; 839 AA.
AC D9VN94;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=Sporulation protein K {ECO:0008006|Google:ProtNLM};
GN ORFNames=SSNG_00852 {ECO:0000313|EMBL:EFL13600.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL13600.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL13600.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL13600.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) 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}.
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DR EMBL; GG657750; EFL13600.1; -; Genomic_DNA.
DR RefSeq; WP_007262549.1; NZ_GG657750.1.
DR AlphaFoldDB; D9VN94; -.
DR STRING; 253839.SSNG_00852; -.
DR eggNOG; COG0464; Bacteria.
DR HOGENOM; CLU_008749_0_0_11; -.
DR Proteomes; UP000005763; 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; 3.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 41..173
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 613..753
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 482..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 839 AA; 87087 MW; 5A0FCE3DE55A52CE CRC64;
MVQGTVQVTH GGTSRWRRRS GEYPTLTAAL AAAVDGDVLS IAPGTYRENL VLRHAVTLRG
PEGSVAGSVR IAPLDGIALT VRASAVVQDL YLEGADRAAP ALLVEEGSPE LTDLRVHTRS
ASGIEVRGGA RPLVRRCTVE NPAGVGISVL DGGGGVFEEC EVVVAGQAGV SVRGGHPRLE
RCRIHHAVGA GIAVTGEGSG LEALGCEVYE VKGTGVQVAA RAAARLTDCA VHRTSADGVT
LDTDAVLTLT GCDIHDIPEN AVDLRSRSVL TLSRTTVRRF GRNGLSVWDP GTRVDAESCE
IHDSTGDYPA VWVSDGATAS LESCRLHDVP DALFVLDRGS RVDVVDSDLS QVRNTAVSVS
DGASAQLDDC RIREAGTGAW FRDHGSGGSL ANCTVDAVQT GVIVTKGADP VLERCTVTSA
AEAGFYVSAG GRGTFTACRV TGSSGFGFHV IDGCRTTLTR CHTERCARGG YEFAEDGPLA
EGCTGDEDGT GPAAGAAGGV LAGARPGGTG PRTATAARDS AGHPADRVPA SRTGAGPDAG
AGAETGTGAG SSAAAQAVPA PAGAGAARGS GEVLGQLDAL VGLDSVKREV RALTDMIEVG
RRRQQAGLKA ASVRRHLVFT GSPGTGKTTV ARLYGEILAA LGVLERGHLV EVSRVDLVGE
HIGSTAIRTQ EAFDRARGGV LFIDEAYALA PEDSGRDFGR EAIDTLVKLM EDHRDAVVVI
VAGYTEEMER FLTVNPGVAS RFSRTITFGD YGPQELLRIV EQQAEEHEYR LGEGTGEALL
KYFTELPKGP AFGNGRTARQ TFEAMVERHA GRVAQLADPG TDELTLLFPE DLPALPAEC
//
