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GP167_BPPH5
ID   GP167_BPPH5             Reviewed;         130 AA.
AC   P15853;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   29-SEP-2021, entry version 55.
DE   RecName: Full=DNA replication protein 16.7;
DE   AltName: Full=Gene product 16.7;
DE            Short=gp16.7;
DE   AltName: Full=Protein p16.7;
GN   Name=16.7;
OS   Bacillus phage phi15 (Bacteriophage phi-15).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX   NCBI_TaxID=10755;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2497055; DOI=10.1016/0378-1119(89)90281-3;
RA   Benes V., Arnold L., Smrt J., Paces V.;
RT   "Nucleotide sequence of the right early region of Bacillus phage phi 15 and
RT   comparison with related phages: reorganization of gene 17 during
RT   evolution.";
RL   Gene 75:341-347(1989).
CC   -!- FUNCTION: Binds to the long stretches of ssDNA of the viral DNA
CC       replication intermediates created during the protein-primed mechanism
CC       of replication of the viral genome and attaches the viral DNA to the
CC       membrane of the infected cells. Required for the redistribution of
CC       replicating viral DNA from the initial replication site to membrane-
CC       associated sites surrounding the nucleoid. Required for the second pull
CC       step of DNA ejection. {ECO:0000250|UniProtKB:P16517}.
CC   -!- SUBUNIT: Homodimer; homooligomer. Interacts with DNA; one dsDNA binding
CC       subunit is constituted by three p16.7 dimers.
CC       {ECO:0000250|UniProtKB:P16517}.
CC   -!- SUBCELLULAR LOCATION: Host cell membrane
CC       {ECO:0000250|UniProtKB:P16517}; Single-pass membrane protein
CC       {ECO:0000250|UniProtKB:P16517}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus gp16.7 family. {ECO:0000305}.
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DR   EMBL; M28830; AAA32332.1; -; Genomic_DNA.
DR   PIR; JS0195; WRBPF5.
DR   SMR; P15853; -.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.8.600; -; 1.
DR   InterPro; IPR009595; Phage_DNA_replic_GP16.7.
DR   InterPro; IPR037211; Phage_DNA_replic_GP16.7_sf.
DR   Pfam; PF06720; Phi-29_GP16_7; 1.
DR   SUPFAM; SSF140713; SSF140713; 1.
PE   3: Inferred from homology;
KW   Coiled coil; DNA replication; DNA-binding; Early protein;
KW   Host cell membrane; Host membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Viral DNA replication.
FT   CHAIN           1..130
FT                   /note="DNA replication protein 16.7"
FT                   /id="PRO_0000106614"
FT   TRANSMEM        1..20
FT                   /note="Helical"
FT                   /evidence="ECO:0000250|UniProtKB:P16517"
FT   REGION          70..130
FT                   /note="DNA-binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16517"
FT   COILED          17..56
FT                   /evidence="ECO:0000255"
FT   SITE            113
FT                   /note="Involved in dimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P16517"
FT   SITE            116
FT                   /note="Involved in dimerization"
FT                   /evidence="ECO:0000250|UniProtKB:P16517"
FT   SITE            120
FT                   /note="Involved in oligomerization and DNA binding"
FT                   /evidence="ECO:0000250|UniProtKB:P16517"
SQ   SEQUENCE   130 AA;  15294 MW;  32FE6F3C847059DC CRC64;
     MEAILMIGVI TLCVIFLLSG RNNKKKQEIR ELEDYLEDLN QRIVQRTQIL SELNEVITNR
     SVDKSVNMSA CEIAVLDLYE QSNIRIPSDI IEDMVNQRLQ SEQDVLNYIE TQRTYWKLEN
     QKKLYRGSLK
 
 
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