CAS4_FRATN
ID CAS4_FRATN Reviewed; 196 AA.
AC A0Q5Y6;
DT 11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
DE RecName: Full=CRISPR-associated exonuclease Cas4;
DE EC=3.1.12.1 {ECO:0000250|UniProtKB:Q97TX9};
GN Name=cas4 {ECO:0000303|PubMed:23584588}; OrderedLocusNames=FTN_0760;
OS Francisella tularensis subsp. novicida (strain U112).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=401614;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U112;
RX PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT "Comparison of Francisella tularensis genomes reveals evolutionary events
RT associated with the emergence of human pathogenic strains.";
RL Genome Biol. 8:R102.1-R102.16(2007).
RN [2]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=U112;
RX PubMed=23584588; DOI=10.1038/nature12048;
RA Sampson T.R., Saroj S.D., Llewellyn A.C., Tzeng Y.L., Weiss D.S.;
RT "A CRISPR/Cas system mediates bacterial innate immune evasion and
RT virulence.";
RL Nature 497:254-257(2013).
RN [3]
RP ERRATUM OF PUBMED:23584588.
RX DOI=10.1038/nature12498;
RA Sampson T.R., Saroj S.D., Llewellyn A.C., Tzeng Y.L., Weiss D.S.;
RL Nature 501:602-602(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 sequences complementary to
CC antecedent mobile elements and target invading nucleic acids. CRISPR
CC clusters are transcribed and processed into CRISPR RNA (crRNA). This
CC may be a 5' to 3' ssDNA exonuclease (By similarity).
CC {ECO:0000250|UniProtKB:Q97TX9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=exonucleolytic cleavage in the 5'- to 3'-direction to yield
CC nucleoside 3'-phosphates.; EC=3.1.12.1;
CC Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC Note=Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
CC {ECO:0000250|UniProtKB:Q97TX9};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q97TX9};
CC Note=Binds 1 [4Fe-4S] cluster per subunit. It may be important for
CC protein stability, since mutation of the Cys that binds the cofactor
CC leads to a colorless, insoluble protein.
CC {ECO:0000250|UniProtKB:Q97TX9};
CC -!- INDUCTION: In culture expression is high during early log phase (1
CC hour), decreases and then rises again in late stationary phase (16
CC hours). During infection of mouse bone marrow-derived macrophages
CC (BMDM) expression is maximal after 2 hours, when the bacteria is
CC expected to be in the phagosome. {ECO:0000269|PubMed:23584588}.
CC -!- DISRUPTION PHENOTYPE: No effect on expression of bacterial lipoprotein
CC FTN_1103. Bacteria are as virulent in mice as wild-type bacteria.
CC {ECO:0000269|PubMed:23584588}.
CC -!- MISCELLANEOUS: Part of a type II CRISPR-Cas system.
CC {ECO:0000305|PubMed:23584588}.
CC -!- SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 family.
CC {ECO:0000305}.
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DR EMBL; CP000439; ABK89651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0Q5Y6; -.
DR SMR; A0Q5Y6; -.
DR EnsemblBacteria; ABK89651; ABK89651; FTN_0760.
DR KEGG; ftn:FTN_0760; -.
DR OMA; CCYRNIC; -.
DR BioCyc; FTUL401614:G1G75-792-MON; -.
DR Proteomes; UP000000762; Chromosome.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.90.320.10; -; 1.
DR InterPro; IPR013343; CRISPR-assoc_prot_Cas4.
DR InterPro; IPR022765; Dna2/Cas4_DUF83.
DR InterPro; IPR011604; PDDEXK-like_dom_sf.
DR InterPro; IPR011335; Restrct_endonuc-II-like.
DR Pfam; PF01930; Cas_Cas4; 1.
DR SUPFAM; SSF52980; SSF52980; 1.
DR TIGRFAMs; TIGR00372; cas4; 1.
PE 2: Evidence at transcript level;
KW Antiviral defense; Exonuclease; Hydrolase; Iron; Iron-sulfur; Manganese;
KW Metal-binding; Nuclease.
FT CHAIN 1..196
FT /note="CRISPR-associated exonuclease Cas4"
FT /id="PRO_0000436106"
FT BINDING 23
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 50
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 90
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 103
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 184
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 187
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
FT BINDING 193
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000250|UniProtKB:Q97TX9"
SQ SEQUENCE 196 AA; 22909 MW; 93581AC1D46364F8 CRC64;
MNMDIFDNDL SIPVNLIRQW CFCPRIVYYQ ELLAIKPNKP LWVAQGEEFH KKVEQLEKRR
SFSRYGLENA IRHFNLSIKS QKYKLHGIVD WVIETDTNVY VVEYKTNPNP NSLGHKLQIA
AYALLVQEYF AKPCKTTFLT SDKKSYEIKI TDELINKLIK TISDILSTLD SGNKPDSSAS
DHQCIQCEYY NFCNDR
