ID   VG31_BPT4               Reviewed;         111 AA.
AC   P17313;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1990, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Capsid assembly protein Gp31;
GN   Name=31;
OS   Enterobacteria phage T4 (Bacteriophage T4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX   NCBI_TaxID=10665;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=D;
RX   PubMed=2362813; DOI=10.1093/nar/18.12.3635;
RA   Prilipov A.G., Mesyanzhinov V.V., Aebi U., Kellenberger E.;
RT   "Cloning and sequencing of bacteriophage T4 genes between map positions
RT   128.3-130.3.";
RL   Nucleic Acids Res. 18:3635-3635(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3072258; DOI=10.1016/0378-1119(88)90332-0;
RA   Nivinskas R., Black L.W.;
RT   "Cloning, sequence, and expression of the temperature-dependent phage T4
RT   capsid assembly gene 31.";
RL   Gene 73:251-257(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2377483; DOI=10.1093/nar/18.14.4280;
RA   Raudonikiene A., Nivinskas R.;
RT   "Nucleotide sequence of bacteriophage T4 gene 31 region.";
RL   Nucleic Acids Res. 18:4280-4280(1990).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1587487; DOI=10.1016/0378-1119(92)90711-w;
RA   Raudonikiene A., Nivinskas R.;
RT   "Gene rIII is the nearest downstream neighbour of bacteriophage T4 gene
RT   31.";
RL   Gene 114:85-90(1992).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12626685; DOI=10.1128/mmbr.67.1.86-156.2003;
RA   Miller E.S., Kutter E., Mosig G., Arisaka F., Kunisawa T., Ruger W.;
RT   "Bacteriophage T4 genome.";
RL   Microbiol. Mol. Biol. Rev. 67:86-156(2003).
RN   [6]
RP   MUTAGENESIS.
RX   PubMed=2311934; DOI=10.1016/0378-1119(90)90109-5;
RA   Keppel F., Lipinska B., Ang D., Georgopoulos C.;
RT   "Mutational analysis of the phage T4 morphogenetic 31 gene, whose product
RT   interacts with the Escherichia coli GroEL protein.";
RL   Gene 86:19-25(1990).
RN   [7]
RP   FUNCTION.
RX   PubMed=7908418; DOI=10.1038/368654a0;
RA   van der Vies S.M., Gatenby A.A., Georgopoulos C.;
RT   "Bacteriophage T4 encodes a co-chaperonin that can substitute for
RT   Escherichia coli GroES in protein folding.";
RL   Nature 368:654-656(1994).
RN   [8]
RP   X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX   PubMed=9244309; DOI=10.1016/s0092-8674(00)80343-8;
RA   Hunt J.F., van der Vies S.M., Henry L., Deisenhofer J.;
RT   "Structural adaptations in the specialized bacteriophage T4 co-chaperonin
RT   Gp31 expand the size of the Anfinsen cage.";
RL   Cell 90:361-371(1997).
CC   -!- FUNCTION: Essential for proper capsid assembly. In absence of Gp31 the
CC       major capsid protein (Gp23) assembles into 'lumps'. Acts as a co-
CC       chaperonin with the host groEL protein. {ECO:0000269|PubMed:7908418}.
CC   -!- SUBUNIT: Homoheptamer. Forms a stable complex with groEL in the
CC       presence of ATP.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X17657; CAA35651.1; -; Genomic_DNA.
DR   EMBL; M37882; AAA32506.1; -; Genomic_DNA.
DR   EMBL; X54536; CAA38405.1; -; Genomic_DNA.
DR   EMBL; M34502; AAA32510.1; -; Genomic_DNA.
DR   EMBL; AF158101; AAD42451.1; -; Genomic_DNA.
DR   PIR; JT0488; VHBPP4.
DR   RefSeq; NP_049825.1; NC_000866.4.
DR   PDB; 1G31; X-ray; 2.30 A; A/B/C/D/E/F/G=1-111.
DR   PDB; 2CGT; EM; 8.20 A; O/P/Q/R/S/T/U=1-111.
DR   PDBsum; 1G31; -.
DR   PDBsum; 2CGT; -.
DR   SMR; P17313; -.
DR   DIP; DIP-59724N; -.
DR   IntAct; P17313; 1.
DR   GeneID; 1258757; -.
DR   KEGG; vg:1258757; -.
DR   EvolutionaryTrace; P17313; -.
DR   Proteomes; UP000009087; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR   GO; GO:0019069; P:viral capsid assembly; IDA:CACAO.
DR   CDD; cd00320; cpn10; 1.
DR   Gene3D; 2.30.33.40; -; 1.
DR   InterPro; IPR020818; Chaperonin_GroES.
DR   InterPro; IPR037124; Chaperonin_GroES_sf.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR016416; Phage_T4_Gp31_GroEL.
DR   Pfam; PF00166; Cpn10; 1.
DR   PIRSF; PIRSF004380; Phage_GroES_Gp31; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; Early protein; Reference proteome;
KW   Viral capsid assembly; Viral release from host cell.
FT   CHAIN           1..111
FT                   /note="Capsid assembly protein Gp31"
FT                   /id="PRO_0000165018"
FT   STRAND          15..20
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   HELIX           25..27
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   HELIX           39..44
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   STRAND          45..54
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   STRAND          68..72
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   HELIX           82..85
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   HELIX           91..93
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   STRAND          98..102
FT                   /evidence="ECO:0007829|PDB:1G31"
FT   HELIX           103..105
FT                   /evidence="ECO:0007829|PDB:1G31"
SQ   SEQUENCE   111 AA;  12079 MW;  D4F75212CB849EFD CRC64;
     MSEVQQLPIR AVGEYVILVS EPAQAGDEEV TESGLIIGKR VQGEVPELCV VHSVGPDVPE
     GFCEVGDLTS LPVGQIRNVP HPFVALGLKQ PKEIKQKFVT CHYKAIPCLY K