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FI_LAMBD
ID   FI_LAMBD                Reviewed;         132 AA.
AC   P03709;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-JUN-2021, entry version 75.
DE   RecName: Full=DNA-packaging protein FI;
GN   Name=Fi; OrderedLocusNames=lambdap09;
OS   Escherichia phage lambda (Bacteriophage lambda).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae; Lambdavirus.
OX   NCBI_TaxID=10710;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=6221115; DOI=10.1016/0022-2836(82)90546-0;
RA   Sanger F., Coulson A.R., Hong G.F., Hill D.F., Petersen G.B.;
RT   "Nucleotide sequence of bacteriophage lambda DNA.";
RL   J. Mol. Biol. 162:729-773(1982).
RN   [2]
RP   FUNCTION.
RX   PubMed=9220002; DOI=10.1046/j.1365-2958.1997.4011769.x;
RA   Murialdo H., Tzamtzis D., Berru M., Fife W.L., Becker A.;
RT   "Mutations in the terminase genes of bacteriophage lambda that bypass the
RT   necessity for FI.";
RL   Mol. Microbiol. 24:937-952(1997).
RN   [3]
RP   STRUCTURE BY NMR OF 72-132, INTERACTION WITH MAJOR CAPSID PROTEIN, AND
RP   MUTAGENESIS OF HIS-92 AND PHE-106.
RX   PubMed=22801427; DOI=10.1074/jbc.m112.378349;
RA   Popovic A., Wu B., Arrowsmith C.H., Edwards A.M., Davidson A.R.,
RA   Maxwell K.L.;
RT   "Structural and biochemical characterization of phage lambda FI protein
RT   (gpFI) reveals a novel mechanism of DNA packaging chaperone activity.";
RL   J. Biol. Chem. 287:32085-32095(2012).
CC   -!- FUNCTION: Stimulates the interaction of procapsid with the terminase-
CC       DNA complex, thereby increasing the overall rate of DNA packaging.
CC       Before packaging, it likely coats the surface of the procapsid through
CC       binding mediated by c-terminal domain. FI presumably dissociates from
CC       the capsid once it inflates upon DNA packaging, and is not present in
CC       the mature virion. {ECO:0000269|PubMed:9220002}.
CC   -!- SUBUNIT: Interacts with major capsid protein via c-terminus.
CC       {ECO:0000269|PubMed:22801427}.
CC   -!- SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000305}.
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DR   EMBL; J02459; AAA96541.1; -; Genomic_DNA.
DR   PIR; E04333; JVBPFL.
DR   RefSeq; NP_040588.1; NC_001416.1.
DR   PDB; 2LSM; NMR; -; A=72-132.
DR   PDBsum; 2LSM; -.
DR   BMRB; P03709; -.
DR   SMR; P03709; -.
DR   IntAct; P03709; 4.
DR   GeneID; 2703483; -.
DR   KEGG; vg:2703483; -.
DR   Proteomes; UP000001711; Genome.
DR   GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0019072; P:viral genome packaging; IDA:UniProtKB.
DR   DisProt; DP01336; -.
DR   Gene3D; 3.40.5.70; -; 1.
DR   InterPro; IPR025147; Packaging_FI.
DR   InterPro; IPR043043; Packaging_FI_C.
DR   Pfam; PF14000; Packaging_FI; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Host cytoplasm; Reference proteome; Viral genome packaging;
KW   Viral release from host cell.
FT   CHAIN           1..132
FT                   /note="DNA-packaging protein FI"
FT                   /id="PRO_0000077685"
FT   REGION          81..132
FT                   /note="Capsid binding"
FT   MUTAGEN         92
FT                   /note="H->A: Complete loss of capsid protein binding."
FT                   /evidence="ECO:0000269|PubMed:22801427"
FT   MUTAGEN         106
FT                   /note="F->A: Partial loss of capsid protein binding."
FT                   /evidence="ECO:0000269|PubMed:22801427"
FT   STRAND          83..89
FT                   /evidence="ECO:0007829|PDB:2LSM"
FT   STRAND          98..101
FT                   /evidence="ECO:0007829|PDB:2LSM"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:2LSM"
FT   STRAND          112..115
FT                   /evidence="ECO:0007829|PDB:2LSM"
FT   HELIX           117..125
FT                   /evidence="ECO:0007829|PDB:2LSM"
FT   STRAND          128..131
FT                   /evidence="ECO:0007829|PDB:2LSM"
SQ   SEQUENCE   132 AA;  14308 MW;  4D7640AC64A97BCA CRC64;
     MTKDELIARL RSLGEQLNRD VSLTGTKEEL ALRVAELKEE LDDTDETAGQ DTPLSRENVL
     TGHENEVGSA QPDTVILDTS ELVTVVALVK LHTDALHATR DEPVAFVLPG TAFRVSAGVA
     AEMTERGLAR MQ
 
 
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