CAS10_MYCTU
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 25-MAY-2022, entry version 110.
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., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT 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., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT 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 palindromic
CC repeat) is an adaptive immune system that provides protection against
CC mobile genetic elements (viruses, transposable elements and conjugative
CC plasmids). CRISPR clusters contain spacers, sequences complementary to
CC antecedent mobile elements, and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). The
CC type III-A Csm effector complex binds crRNA and acts as a crRNA-guided
CC RNase, DNase and cyclic oligoadenylate synthase; binding of target RNA
CC cognate to the crRNA is required for all activities (Probable). This
CC CRISPR-Cas system protects bacteria against transformation with
CC plasmids containing DNA homologous to its spacer regions
CC (PubMed:29979631). {ECO:0000269|PubMed:29979631,
CC ECO:0000305|PubMed:29979631}.
CC -!- FUNCTION: This subunit is a single-strand-specific deoxyribonuclease
CC (ssDNase) which digests both linear and circular ssDNA; it has both
CC exo- and endonuclease activity. {ECO:0000250|UniProtKB:B6YWB8}.
CC -!- FUNCTION: ssDNase activity is stimulated in the ternary Csm effector
CC complex; binding of cognate target RNA activates the ssDNase, as the
CC target RNA is degraded ssDNA activity decreases.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- FUNCTION: When associated with the ternary Csm effector complex (the
CC crRNA, Cas proteins and a cognate target ssRNA) synthesizes cyclic
CC oligoadenylates (cOA) from ATP. cOAs are second messengers that
CC stimulate the ssRNase activity of Csm6, inducing an antiviral state
CC 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, Csm2,
CC Csm3, Csm4, Csm5 and mature crRNA. {ECO:0000269|PubMed:29979631}.
CC -!- DOMAIN: The N-terminal HD domain has ssDNase activity. The C-terminal
CC GGDEF domain has the cOA synthesis activity.
CC {ECO:0000250|UniProtKB:A0A0A7HFE1}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the entire CRISPR-Cas locus (cas6 to
CC cas2, Rv2824c to Rv2816c) decreases resistance to plasmids encoding
CC spacer elements about 6-fold. {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}.
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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 PDB; 6KBD; X-ray; 3.00 A; A=534-809.
DR PDB; 6KC0; X-ray; 2.29 A; A=534-809.
DR PDBsum; 6KBD; -.
DR PDBsum; 6KC0; -.
DR AlphaFoldDB; P71629; -.
DR SMR; P71629; -.
DR STRING; 83332.Rv2823c; -.
DR PaxDb; P71629; -.
DR DNASU; 887735; -.
DR GeneID; 887735; -.
DR KEGG; mtu:Rv2823c; -.
DR TubercuList; Rv2823c; -.
DR eggNOG; COG1353; Bacteria.
DR InParanoid; P71629; -.
DR OMA; PSAFYYS; -.
DR PhylomeDB; P71629; -.
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 CDD; cd09680; Cas10_III; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR InterPro; IPR013408; Cas10/Csm1.
DR InterPro; IPR041062; Csm1_B.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR Pfam; PF18211; Csm1_B; 1.
DR TIGRFAMs; TIGR02578; cas_TM1811_Csm1; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; Endonuclease; Exonuclease;
KW Hydrolase; Nuclease; Nucleotide-binding; Reference proteome; RNA-binding;
KW Transferase.
FT CHAIN 1..809
FT /note="CRISPR system single-strand-specific
FT deoxyribonuclease Cas10/Csm1 (subtype III-A)"
FT /id="PRO_0000418224"
FT DOMAIN 1..98
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 547..700
FT /note="GGDEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00095"
FT STRAND 549..556
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 578..593
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 595..601
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 611..613
FT /evidence="ECO:0007829|PDB:6KBD"
FT STRAND 618..625
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 628..634
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 635..652
FT /evidence="ECO:0007829|PDB:6KC0"
FT TURN 653..655
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 659..666
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 672..687
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 689..691
FT /evidence="ECO:0007829|PDB:6KBD"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 706..711
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 712..716
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 717..723
FT /evidence="ECO:0007829|PDB:6KC0"
FT TURN 724..727
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 732..740
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 756..759
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 773..782
FT /evidence="ECO:0007829|PDB:6KC0"
FT STRAND 783..786
FT /evidence="ECO:0007829|PDB:6KC0"
FT HELIX 788..803
FT /evidence="ECO:0007829|PDB:6KC0"
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
