ID CAS10_MYCTU Reviewed; 809 AA. AC P71629; L0TDG3; DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 13-FEB-2019, entry version 98. DE RecName: Full=CRISPR system single-strand-specific deoxyribonuclease Cas10/Csm1 (subtype III-A); DE Short=ssDNase Cas10; DE EC=3.1.-.-; DE AltName: Full=Cyclic oligoadenylate synthase; DE EC=2.7.7.- {ECO:0000250|UniProtKB:A0A0A7HFE1}; GN Name=cas10; Synonyms=csm1; OrderedLocusNames=Rv2823c; OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv). OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=83332; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=9634230; DOI=10.1038/31159; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., RA Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, RA Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T., RA Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S., RA Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A., RA Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC STRAIN=ATCC 25618 / H37Rv; RX PubMed=21969609; DOI=10.1074/mcp.M111.011627; RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., RA Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H., RA Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., RA Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S., RA Dash D., Pandey A.; RT "Proteogenomic analysis of Mycobacterium tuberculosis by high RT resolution mass spectrometry."; RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011). RN [3] RP FUNCTION IN PLASMID RESISTANCE, SUBUNIT, AND DISRUPTION PHENOTYPE. RC STRAIN=H37Rv; RX PubMed=29979631; DOI=10.1096/fj.201800557RR; RA Wei W., Zhang S., Fleming J., Chen Y., Li Z., Fan S., Liu Y., Wang W., RA Wang T., Liu Y., Ren B., Wang M., Jiao J., Chen Y., Zhou Y., Zhou Y., RA Gu S., Zhang X., Wan L., Chen T., Zhou L., Chen Y., Zhang X.E., Li C., RA Zhang H., Bi L.; RT "Mycobacterium tuberculosis type III-A CRISPR/Cas system crRNA and its RT maturation have atypical features."; RL FASEB J. 33:1496-1509(2019). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA). The type III-A Csm effector CC complex binds crRNA and acts as a crRNA-guided RNase, DNase and CC cyclic oligoadenylate synthase; binding of target RNA cognate to CC the crRNA is required for all activities (Probable). This CRISPR- CC Cas system protects bacteria against transformation with plasmids CC containing DNA homologous to its spacer regions (PubMed:29979631). CC {ECO:0000269|PubMed:29979631, ECO:0000305|PubMed:29979631}. CC -!- FUNCTION: This subunit is a single-strand-specific CC deoxyribonuclease (ssDNase) which digests both linear and circular CC ssDNA; it has both exo- and endonuclease activity. CC {ECO:0000250|UniProtKB:B6YWB8}. CC -!- FUNCTION: ssDNase activity is stimulated in the ternary Csm CC effector complex; binding of cognate target RNA activates the CC ssDNase, as the target RNA is degraded ssDNA activity decreases. CC {ECO:0000250|UniProtKB:A0A0A7HFE1}. CC -!- FUNCTION: When associated with the ternary Csm effector complex CC (the crRNA, Cas proteins and a cognate target ssRNA) synthesizes CC cyclic oligoadenylates (cOA) from ATP. cOAs are second messengers CC that stimulate the ssRNase activity of Csm6, inducing an antiviral CC state important for defense against invading nucleic acids. CC {ECO:0000250|UniProtKB:A0A0A7HFE1}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:A0A0A7HFE1}; CC -!- SUBUNIT: Part of the Csm effector complex, that includes Cas10, CC Csm2, Csm3, Csm4, Csm5 and mature crRNA. CC {ECO:0000269|PubMed:29979631}. CC -!- DOMAIN: The N-terminal HD domain has ssDNase activity. The C- CC terminal GGDEF domain has the cOA synthesis activity. CC {ECO:0000250|UniProtKB:A0A0A7HFE1}. CC -!- DISRUPTION PHENOTYPE: Deletion of the entire CRISPR-Cas locus CC (cas6 to cas2, Rv2824c to Rv2816c) decreases resistance to CC plasmids encoding spacer elements about 6-fold. CC {ECO:0000269|PubMed:29979631}. CC -!- MISCELLANEOUS: Encoded in a type III-A CRISPR locus. CC {ECO:0000305|PubMed:29979631}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Cas10/Csm1 family. CC {ECO:0000305}. 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; AL123456; CCP45623.1; -; Genomic_DNA. DR PIR; B70692; B70692. DR RefSeq; NP_217339.1; NC_000962.3. DR RefSeq; WP_003911999.1; NZ_NVQJ01000006.1. DR ProteinModelPortal; P71629; -. DR STRING; 83332.Rv2823c; -. DR PaxDb; P71629; -. DR PRIDE; P71629; -. DR EnsemblBacteria; CCP45623; CCP45623; Rv2823c. DR GeneID; 887735; -. DR KEGG; mtu:Rv2823c; -. DR TubercuList; Rv2823c; -. DR eggNOG; ENOG410695F; Bacteria. DR eggNOG; COG1353; LUCA. DR HOGENOM; HOG000220575; -. DR InParanoid; P71629; -. DR KO; K07016; -. DR OMA; LKMDVDN; -. DR PhylomeDB; P71629; -. DR BioCyc; MTBH37RV:G185E-7073-MONOMER; -. DR Proteomes; UP000001584; Chromosome. DR GO; GO:0005576; C:extracellular region; HDA:MTBBASE. DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR013408; CRISPR-assoc_prot_Csm1. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR003607; HD/PDEase_dom. DR TIGRFAMs; TIGR02578; cas_TM1811_Csm1; 1. DR PROSITE; PS50887; GGDEF; 1. DR PROSITE; PS51831; HD; 1. PE 1: Evidence at protein level; KW Antiviral defense; ATP-binding; Complete proteome; Endonuclease; KW Exonuclease; Hydrolase; Nuclease; Nucleotide-binding; KW Reference proteome; RNA-binding; Transferase. FT CHAIN 1 809 CRISPR system single-strand-specific FT deoxyribonuclease Cas10/Csm1 (subtype FT III-A). FT /FTId=PRO_0000418224. FT DOMAIN 1 98 HD. {ECO:0000255|PROSITE- FT ProRule:PRU01175}. FT DOMAIN 547 700 GGDEF. {ECO:0000255|PROSITE- FT ProRule:PRU00095}. SQ SEQUENCE 809 AA; 90747 MW; E7328ED485D73531 CRC64; MNPQLIEAII GCLLHDIGKP VQRAALGYPG RHSAIGRAFM KKVWLRDSRN PSQFTDEVDE ADIGVSDRRI LDAISYHHSS ALRTAAENGR LAADAPAYIA YNIAAGTDRR KADSDDGHGA STWDPDTPLY SMFNRFGSGT ANLAFAPEML DDRKPINIPS PRRIEFDKDR YAAIVNKLKA ILVDLERSDT YLASLLNVLE ATLSFVPSST DASEVVDVSL FDHLKLTGAL GACIWHYLQA TGQSDFKSAL FDKQDTFYNE KAFLLTTFDV SGIQDFIYTI HSSGAAKMLR ARSFYLEMLT EHLIDELLAR VGLSRANLNY SGGGHAYLLL PNTESARKSV EQFEREANDW LLENFATRLF IATGSVPLAA NDLMRRPNES ASQASNRALR YSGLYRELSE QLSAKKLARY SADQLRELNS RDHDGQKGDR ECSVCHTVNR TVSADDEPKC SLCQALTAAS SQIQSESRRF LLISDGATKG LPLPFGATLT FCSRADADKA LQQPQTRRRY AKNKFFAGEC LGTGLWVGDY VAQMEFGDYV KRASGIARLG VLRLDVDNLG QAFTHGFMEQ GNGKFNTISR TAAFSRMLSL FFRQHINYVL ARPKLRPITG DDPARPREAT IIYSGGDDVF VVGAWDDVIE FGIELRERFH EFTQGKLTVS AGIGMFPDKY PISVMAREVG DLEDAAKSLP GKNGVALFDR EFTFGWDELL SKVIEEKYRH IADYFSGNEE RGMAFIYKLL ELLAERDDRI TKARWVYFLT RMRNPTGDTA PFQQFANRLH QWFQDPTDAK QLKTALHLYI YRTRKEESE //