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