CAP6_ECOM1
ID CAP6_ECOM1 Reviewed; 311 AA.
AC D7Y2H4;
DT 10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 32.
DE RecName: Full=CD-NTase-associated protein 6 {ECO:0000303|PubMed:32839535};
DE Short=Cap6 {ECO:0000303|PubMed:32839535};
DE AltName: Full=CBASS disassembly protein Trip13 {ECO:0000303|PubMed:31932165};
DE AltName: Full=Probable ATPase Trip13 {ECO:0000303|PubMed:31932165};
GN Name=cap6 {ECO:0000303|PubMed:32839535};
GN Synonyms=trip13 {ECO:0000303|PubMed:31932165};
GN ORFNames=HMPREF9540_01760 {ECO:0000312|EMBL:EFJ98158.1};
OS Escherichia coli (strain MS 115-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=749537;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MS 115-1;
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA Chinwalla A., Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP CLASSIFICATION AND NOMENCLATURE.
RX PubMed=32839535; DOI=10.1038/s41564-020-0777-y;
RA Millman A., Melamed S., Amitai G., Sorek R.;
RT "Diversity and classification of cyclic-oligonucleotide-based anti-phage
RT signalling systems.";
RL Nat. Microbiol. 5:1608-1615(2020).
RN [3] {ECO:0007744|PDB:6P8V}
RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 3-308 IN COMPLEX WITH CDNC AND
RP CAP7, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LYS-87 AND GLU-159.
RC STRAIN=MS 115-1;
RX PubMed=31932165; DOI=10.1016/j.molcel.2019.12.009;
RA Ye Q., Lau R.K., Mathews I.T., Birkholz E.A., Watrous J.D., Azimi C.S.,
RA Pogliano J., Jain M., Corbett K.D.;
RT "HORMA Domain Proteins and a Trip13-like ATPase Regulate Bacterial cGAS-
RT like Enzymes to Mediate Bacteriophage Immunity.";
RL Mol. Cell 77:709-722(2020).
CC -!- FUNCTION: CBASS (cyclic oligonucleotide-based antiphage signaling
CC system) provides immunity against bacteriophage. The CD-NTase protein
CC synthesizes cyclic nucleotides in response to infection; these serve as
CC specific second messenger signals. The signals activate a diverse range
CC of effectors, leading to bacterial cell death and thus abortive phage
CC infection. A type III-C(AAA) CBASS system (PubMed:32839535).
CC {ECO:0000269|PubMed:31932165, ECO:0000303|PubMed:32839535}.
CC -!- FUNCTION: Binds and disassembles an active CdnC:Cap7 (Cap7 is also
CC called HORMA) complex, inhibiting the complex's ability to synthesize
CC cyclic nucleotide second messengers (PubMed:31932165). An AAA+-ATPase
CC remodeler, it is thought that in the absence of foreign threat Cap6
CC (also called Trip13) maintains the Cap7 protein in its open, inactive
CC state. Once activated (presumably by a bacteriophage protein) Cap7
CC binds to and activates its cognate CD-NTase (CdnC in this bacteria) to
CC synthesize cAAA, a cyclic nucleotide second messenger. cAAA activates
CC the NucC endonuclease which degrades all DNA in the infected cell,
CC causing cell death and abortive phage infection (Probable).
CC {ECO:0000269|PubMed:31932165, ECO:0000305|PubMed:31932165}.
CC -!- FUNCTION: Protects E.coli strain JP313 against bacteriophage lambda
CC cI- infection. When the cdnC-cap7-cap6-nucC operon is transformed into
CC a susceptible E.coli strain it confers bacteriophage lambda
CC cI- immunity. Mutations in the sensor (Cap7 also called HORMA) or
CC effector proteins (CdnC, NucC) but not the disassembly protein (Cap6
CC also called Trip13) no longer confer immunity. The presence of the
CC intact operon leads to culture collapse and cell death, which occurs
CC before the phage has finished its replication cycle, thus protecting
CC non-infected bacteria by aborting the phage infection and preventing
CC its propagation. {ECO:0000269|PubMed:31932165}.
CC -!- SUBUNIT: Homohexamer. Forms a 1:1:6 CdnC:Cap7:Cap6 complex.
CC {ECO:0000269|PubMed:31932165}.
CC -!- DOMAIN: In the disassembly complex (PDB:6P8V) Cap6 (this protein)
CC crystallizes as a right-handed spiral; the top 4 subunits bind ATP
CC while the bottom 2 do not. A CdnC monomer lies along the surface of the
CC hexamer at the interface of subunits 5 and 6, with Cap7 (also called
CC HORMA) at its tip, over the central hexamer pore. The N-terminus of
CC Cap7 extends into the pore, contacting 5/6 Cap6 subunits.
CC {ECO:0000269|PubMed:31932165}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; ADTL01000141; EFJ98158.1; -; Genomic_DNA.
DR RefSeq; WP_001101343.1; NZ_GG771785.1.
DR PDB; 6P8V; X-ray; 2.64 A; A/B/C/D/E/F=3-308.
DR PDBsum; 6P8V; -.
DR AlphaFoldDB; D7Y2H4; -.
DR SMR; D7Y2H4; -.
DR EnsemblBacteria; EFJ98158; EFJ98158; HMPREF9540_01760.
DR HOGENOM; CLU_058955_0_0_6; -.
DR Proteomes; UP000032708; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; ATP-binding; Nucleotide-binding.
FT CHAIN 1..311
FT /note="CD-NTase-associated protein 6"
FT /id="PRO_0000451843"
FT BINDING 84..89
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:31932165,
FT ECO:0007744|PDB:6P8V"
FT BINDING 215..216
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:31932165,
FT ECO:0007744|PDB:6P8V"
FT MUTAGEN 87
FT /note="K->A: Partially inhibits second messenger synthesis
FT by CdnC:Cap7:DNA complex."
FT /evidence="ECO:0000269|PubMed:31932165"
FT MUTAGEN 159
FT /note="E->Q: Stabilizes a 1:1:6 CdnC:Cap7:Cap6 complex,
FT probably prevents ATP hydrolysis. Still confers phage
FT immunity."
FT /evidence="ECO:0000269|PubMed:31932165"
FT HELIX 7..11
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 15..18
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 20..28
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 105..111
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 160..163
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 174..192
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 196..204
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 211..216
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 228..239
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:6P8V"
FT STRAND 259..263
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 268..272
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 275..283
FT /evidence="ECO:0007829|PDB:6P8V"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:6P8V"
FT HELIX 291..300
FT /evidence="ECO:0007829|PDB:6P8V"
SQ SEQUENCE 311 AA; 34358 MW; 745DAF9F1763971B CRC64;
MNVKPSLDEL FERRINFPDF EPQERLARLV GLDEHKDRLS KILGLLVNPY GIQEWAKKYH
PDARAAVDTV LRRPPLVVLA GDVGSGKTEL AETIGDAVAR QEDIDITLYP LSLATRGQGR
VGEMTQLVSA AFDYTIEAAD KLKNTNGKAR GAVLLLIDEA DALAQSRENA QMHHEDRAGV
NAFIRGIDRI ANQKLPAAVL MCTNRLKALD PAVQRRAAEI LTFSRPNDEQ RHYLLHSKLT
GLGLNSTAVE ELVRLTGPRD PNSPGFTFSD ITQRLIPSII LAAYPYNAVS VHSALQVVNK
MTPTPAFIDR Q
