HOC_BPT4
ID HOC_BPT4 Reviewed; 376 AA.
AC P18056;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 29-SEP-2021, entry version 106.
DE RecName: Full=Highly immunogenic outer capsid protein {ECO:0000255|HAMAP-Rule:MF_04116};
DE Short=Hoc;
GN Name=hoc;
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].
RX PubMed=2377482; DOI=10.1093/nar/18.14.4277;
RA Kaliman A.V., Khasanova M.A., Kryukov V.M., Tanyashin V.I., Bayev A.A.;
RT "The nucleotide sequence of the region of bacteriophage T4 inh(lip)-hoc
RT genes.";
RL Nucleic Acids Res. 18:4277-4277(1990).
RN [2]
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 [3]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH THE MAJOR CAPSID PROTEIN.
RX PubMed=1469720; DOI=10.1016/0022-2836(92)90871-g;
RA Steven A.C., Greenstone H.L., Booy F.P., Black L.W., Ross P.D.;
RT "Conformational changes of a viral capsid protein. Thermodynamic rationale
RT for proteolytic regulation of bacteriophage T4 capsid expansion, co-
RT operativity, and super-stabilization by soc binding.";
RL J. Mol. Biol. 228:870-884(1992).
RN [4]
RP REVIEW.
RX PubMed=21129201; DOI=10.1186/1743-422x-7-356;
RA Rao V.B., Black L.W.;
RT "Structure and assembly of bacteriophage T4 head.";
RL Virol. J. 7:356-356(2010).
RN [5]
RP INTERACTION WITH THE MAJOR CAPSID PROTEIN.
RX PubMed=20497329; DOI=10.1111/j.1365-2958.2010.07219.x;
RA Sathaliyawala T., Islam M.Z., Li Q., Fokine A., Rossmann M.G., Rao V.B.;
RT "Functional analysis of the highly antigenic outer capsid protein, Hoc, a
RT virus decoration protein from T4-like bacteriophages.";
RL Mol. Microbiol. 77:444-455(2010).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (22.0 ANGSTROMS), FUNCTION, AND
RP SUBCELLULAR LOCATION.
RX PubMed=15071181; DOI=10.1073/pnas.0400444101;
RA Fokine A., Chipman P.R., Leiman P.G., Mesyanzhinov V.V., Rao V.B.,
RA Rossmann M.G.;
RT "Molecular architecture of the prolate head of bacteriophage T4.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:6003-6008(2004).
RN [7]
RP STRUCTURE BY ELECTRON MICROSCOPY (15.0 ANGSTROMS), INTERACTION WITH THE
RP MAJOR CAPSID PROTEIN, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11162794; DOI=10.1006/viro.2000.0735;
RA Olson N.H., Gingery M., Eiserling F.A., Baker T.S.;
RT "The structure of isometric capsids of bacteriophage T4.";
RL Virology 279:385-391(2001).
CC -!- FUNCTION: Capsid decoration protein that binds as a monomer at the
CC center of each major capsid protein hexamer once maturation and
CC expension of the capsid has occured. It only has a marginal effect on
CC head stability. Dispensable for the head morphogenesis and phage
CC infection. {ECO:0000255|HAMAP-Rule:MF_04116,
CC ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:1469720,
CC ECO:0000269|PubMed:15071181}.
CC -!- SUBUNIT: Monomer (PubMed:1469720). Interacts with the major capsid
CC protein; one hoc molecule associates with each hexamer facet
CC (PubMed:1469720, PubMed:11162794, PubMed:20497329). {ECO:0000255|HAMAP-
CC Rule:MF_04116, ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:1469720,
CC ECO:0000269|PubMed:20497329}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000255|HAMAP-Rule:MF_04116,
CC ECO:0000269|PubMed:11162794, ECO:0000269|PubMed:15071181}. Note=The Hoc
CC protein is the most prominent feature at the virion surface. There are
CC 155 copies on the capsid. {ECO:0000269|PubMed:15071181}.
CC -!- SIMILARITY: Belongs to the Tevenvirinae Hoc family. {ECO:0000255|HAMAP-
CC Rule:MF_04116}.
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DR EMBL; X14869; CAA33010.1; -; Genomic_DNA.
DR EMBL; AF158101; AAD42581.1; -; Genomic_DNA.
DR PIR; JQ0566; ZXBPH4.
DR RefSeq; NP_049793.1; NC_000866.4.
DR PDB; 5VF3; EM; 3.30 A; Z=1-376.
DR PDBsum; 5VF3; -.
DR SMR; P18056; -.
DR GeneID; 1258642; -.
DR KEGG; vg:1258642; -.
DR Proteomes; UP000009087; Genome.
DR GO; GO:0098021; C:viral capsid, decoration; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.10; -; 2.
DR HAMAP; MF_04116; HOC_T4; 1.
DR InterPro; IPR038998; HOC.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR Pfam; PF00801; PKD; 1.
DR SMART; SM00089; PKD; 2.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49299; SSF49299; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Capsid protein; Reference proteome; Virion.
FT CHAIN 1..376
FT /note="Highly immunogenic outer capsid protein"
FT /id="PRO_0000164945"
FT REGION 355..359
FT /note="Interaction with the major capsid protein"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04116,
FT ECO:0000269|PubMed:20497329"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:5VF3"
FT TURN 319..322
FT /evidence="ECO:0007829|PDB:5VF3"
SQ SEQUENCE 376 AA; 40387 MW; B5595931DCB319EC CRC64;
MTFTVDITPK TPTGVIDETK QFTATPSGQT GGGTITYAWS VDNVPQDGAE ATFSYVLKGP
AGQKTIKVVA TNTLSEGGPE TAEATTTITV KNKTQTTTLA VTPASPAAGV IGTPVQFTAA
LASQPDGASA TYQWYVDDSQ VGGETNSTFS YTPTTSGVKR IKCVAQVTAT DYDALSVTSN
EVSLTVNKKT MNPQVTLTPP SINVQQDASA TFTANVTGAP EEAQITYSWK KDSSPVEGST
NVYTVDTSSV GSQTIEVTAT VTAADYNPVT VTKTGNVTVT AKVAPEPEGE LPYVHPLPHR
SSAYIWCGWW VMDEIQKMTE EGKDWKTDDP DSKYYLHRYT LQKMMKDYPE VDVQESRNGY
IIHKTALETG IIYTYP
