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CAP7_ECOM1
ID   CAP7_ECOM1              Reviewed;         172 AA.
AC   D7Y2H3;
DT   10-FEB-2021, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2021, sequence version 2.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=CD-NTase-associated protein 7 {ECO:0000303|PubMed:32839535};
DE            Short=Cap7 {ECO:0000303|PubMed:32839535};
DE   AltName: Full=Bacterial HORMA sensor protein {ECO:0000303|PubMed:31932165};
GN   Name=cap7 {ECO:0000303|PubMed:32839535};
GN   Synonyms=HORMA1 {ECO:0000303|PubMed:31932165};
GN   ORFNames=HMPREF9540_01759 {ECO:0000312|EMBL:EFJ98157.1};
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, ECO:0007744|PDB:6U7B}
RP   X-RAY CRYSTALLOGRAPHY (2.09 ANGSTROMS) OF 13-172 IN COMPLEX WITH CDNC AND
RP   WITH CLOSURE PEPTIDE, X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 2-172 IN
RP   COMPLEX WITH CDNC AND CAP6, FUNCTION, INTERACTION WITH CDNC, SUBUNIT,
RP   DOMAIN, AND MUTAGENESIS OF 1-MET--GLN-12; 32-ARG--ARG-35; ARG-32 AND
RP   ARG-35.
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: The sensor protein for this CBASS system. Binds to a closure
CC       peptide (consensus His-Xaa-Xaa-Ile-Leu-Leu-Thr), which allows it to
CC       activate CdnC for second messenger synthesis.
CC       {ECO:0000269|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 strain it confers bacteriophage immunity. Mutations in
CC       the sensor (Cap7 also called HORMA) or effector proteins (CdnC, NucC)
CC       but not the disassembly protein (Cap6 also called Trip13) no longer
CC       confer immunity. The presence of the intact operon leads to culture
CC       collapse and cell death, which occurs before the phage has finished its
CC       replication cycle, thus protecting non-infected bacteria by aborting
CC       the phage infection and preventing its propagation.
CC       {ECO:0000269|PubMed:31932165}.
CC   -!- SUBUNIT: Forms complexes with CdnC with 1:1 and 2:2 stoichimetry, and a
CC       1:1:6 CdnC:Cap7:Cap6 complex. {ECO:0000269|PubMed:31932165}.
CC   -!- DOMAIN: In the disassembly complex (PDB:6P8V) Cap6 (also called Trip13)
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 (this protein)
CC       at its tip, over the central hexamer pore. The N-terminus of Cap7
CC       extends into the pore, contacting 5/6 Cap6 subunits.
CC       {ECO:0000269|PubMed:31932165}.
CC   -!- SIMILARITY: Belongs to the bacterial HORMA family. HORMA1 subfamily.
CC       {ECO:0000305|PubMed:31932165}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EFJ98157.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; ADTL01000141; EFJ98157.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000100572.1; NZ_GG771785.1.
DR   PDB; 6P8V; X-ray; 2.64 A; H=2-172.
DR   PDB; 6U7B; X-ray; 2.09 A; B/D=13-172.
DR   PDBsum; 6P8V; -.
DR   PDBsum; 6U7B; -.
DR   AlphaFoldDB; D7Y2H3; -.
DR   SMR; D7Y2H3; -.
DR   EnsemblBacteria; EFJ98157; EFJ98157; HMPREF9540_01759.
DR   HOGENOM; CLU_1561678_0_0_6; -.
DR   Proteomes; UP000032708; Unassembled WGS sequence.
DR   GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR   InterPro; IPR041162; Bact_HORMA_1.
DR   Pfam; PF18138; bacHORMA_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antiviral defense.
FT   CHAIN           1..172
FT                   /note="CD-NTase-associated protein 7"
FT                   /id="PRO_0000451840"
FT   REGION          141..172
FT                   /note="Required for binding to CdnC and to confer phage
FT                   immunity"
FT                   /evidence="ECO:0000269|PubMed:31932165"
FT   MUTAGEN         1..12
FT                   /note="Missing: Fully active in second messenger formation.
FT                   Cap7:CdnC complex is no longer disassembled by Cap6."
FT                   /evidence="ECO:0000269|PubMed:31932165"
FT   MUTAGEN         32..35
FT                   /note="RMQR->AMQA: No longer binds to CdnC. No longer
FT                   confers phage immunity."
FT                   /evidence="ECO:0000269|PubMed:31932165"
FT   MUTAGEN         32
FT                   /note="R->A: Binds to CdnC."
FT                   /evidence="ECO:0000269|PubMed:31932165"
FT   MUTAGEN         35
FT                   /note="R->A: Binds to CdnC."
FT                   /evidence="ECO:0000269|PubMed:31932165"
FT   HELIX           16..37
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   HELIX           42..58
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   STRAND          61..70
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   STRAND          73..85
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   STRAND          108..115
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   HELIX           117..121
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   HELIX           124..130
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   TURN            131..133
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   STRAND          139..141
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   STRAND          145..158
FT                   /evidence="ECO:0007829|PDB:6U7B"
FT   STRAND          161..169
FT                   /evidence="ECO:0007829|PDB:6U7B"
SQ   SEQUENCE   172 AA;  19144 MW;  1B7E2104ACDB2D44 CRC64;
     MSSYSYTVAE TQTFSVTHAR HMAAKVATDL RRMQRFYGYP SDADIEAYEE ELVVFLKAGY
     LGEVSYGFQK NNNWIEPTLR YTAGDLLGSG TDDDPGKIRP GKDVSGASFY SFMTYSSKYL
     NATQSEKDTA LKDLPFKRVG AQSPGINGYL ENDKTYSAGG RSLTRTSVRN FV
 
 
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