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 02-SEP-2026, entry version 134. DE RecName: Full=Capsid assembly protein Gp31; GN Name=31; OS Enterobacteria phage T4 (Bacteriophage T4). OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Pantevenvirales; Straboviridae; 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 SMR; P17313; -. DR DIP; DIP-59724N; -. DR IntAct; P17313; 1. DR GeneID; 1258757; -. DR KEGG; vg:1258757; -. DR OrthoDB; 19822at10239; -. DR EvolutionaryTrace; P17313; -. DR Proteomes; UP000009087; Segment. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0044183; F:protein folding chaperone; IEA:InterPro. DR GO; GO:0019069; P:viral capsid assembly; IDA:CACAO. DR CDD; cd00320; cpn10; 1. DR FunFam; 2.30.33.40:FF:000006; Head assembly cochaperone with GroEL; 1. DR Gene3D; 2.30.33.40; GroES chaperonin; 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; GroES-like; 1. DR PDBsum; 1G31; -. DR PDBsum; 2CGT; -. 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 35..38 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 //