ID   CSA5A_SACS2             Reviewed;         162 AA.
AC   Q97YC8;
DT   16-MAR-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=CRISPR type I-A cluster 1/Apern-associated protein Csa5-1;
GN   Name=csa5; OrderedLocusNames=SSO1398;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.72 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF ASP-35.
RX   PubMed=23846216; DOI=10.4161/rna.23854;
RA   Reeks J., Graham S., Anderson L., Liu H., White M.F., Naismith J.H.;
RT   "Structure of the archaeal Cascade subunit Csa5: relating the small
RT   subunits of CRISPR effector complexes.";
RL   RNA Biol. 10:762-769(2013).
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).
CC       {ECO:0000305}.
CC   -!- SUBUNIT: Oligomerizes as an infinite helical thread in crystal
CC       structure; disrupting a potential salt bridge between Asp-35 and Arg-55
CC       leads to altered elution from a sizing column. By immunoprecipitation
CC       Csa5 interacts weakly with a Cas5/Cas7 complex. There are 3 csa5, 3
CC       cas5 and 2 cas7 genes in this organism; the immunoprecipitation studies
CC       may not distinguish between them. {ECO:0000269|PubMed:23846216}.
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DR   EMBL; AE006641; AAK41633.1; -; Genomic_DNA.
DR   PIR; B99297; B99297.
DR   RefSeq; WP_009988390.1; NC_002754.1.
DR   PDB; 3ZC4; X-ray; 2.72 A; A/B/C/D/E/F/G/H/I=1-162.
DR   PDBsum; 3ZC4; -.
DR   AlphaFoldDB; Q97YC8; -.
DR   SMR; Q97YC8; -.
DR   STRING; 273057.SSO1398; -.
DR   EnsemblBacteria; AAK41633; AAK41633; SSO1398.
DR   GeneID; 44130254; -.
DR   KEGG; sso:SSO1398; -.
DR   PATRIC; fig|273057.12.peg.1414; -.
DR   eggNOG; arCOG03823; Archaea.
DR   HOGENOM; CLU_1631728_0_0_2; -.
DR   OMA; YIVTPRR; -.
DR   Proteomes; UP000001974; Chromosome.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense; Reference proteome.
FT   CHAIN           1..162
FT                   /note="CRISPR type I-A cluster 1/Apern-associated protein
FT                   Csa5-1"
FT                   /id="PRO_0000435656"
FT   MUTAGEN         35
FT                   /note="D->A: Altered protein oligomerization, protein has a
FT                   smaller radius of gyration, elution from a sizing column is
FT                   altered."
FT                   /evidence="ECO:0000269|PubMed:23846216"
FT   HELIX           7..14
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           16..27
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           31..33
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           35..39
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           43..63
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          65..72
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          79..89
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           98..101
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   TURN            103..105
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          106..109
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          115..117
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          120..123
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          126..129
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           134..146
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   HELIX           149..159
FT                   /evidence="ECO:0007829|PDB:3ZC4"
FT   STRAND          160..162
FT                   /evidence="ECO:0007829|PDB:3ZC4"
SQ   SEQUENCE   162 AA;  18523 MW;  12622E57398E516B CRC64;
     MEASEPVAET ISKRFWTLIK MLRFYVVLRR FGYIDPLIYS IDPKQIKDVL SEALREFVSY
     TSSSSSRSIV IYDDPKNPVT AQAPCLVVAK RDEIPQNFPS IYRYTIYKID KSSEYCISPL
     VVNDKYATLI TPNESVIKEF FDKLDSNIQY ARVLASLAVG GE