ID   H_BPPHS                 Reviewed;         328 AA.
AC   P03646;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   02-JUN-2021, entry version 99.
DE   RecName: Full=Minor spike protein H;
DE   AltName: Full=H protein;
DE   AltName: Full=Pilot protein;
GN   Name=H;
OS   Enterobacteria phage phiX174 (Isolate Sanger) (Bacteriophage phi-X174).
OC   Viruses; Monodnaviria; Sangervirae; Phixviricota; Malgrandaviricetes;
OC   Petitvirales; Microviridae; Bullavirinae; Sinsheimervirus.
OX   NCBI_TaxID=1217068;
OH   NCBI_TaxID=498388; Escherichia coli C.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=870828; DOI=10.1038/265687a0;
RA   Sanger F., Air G.M., Barrell B.G., Brown N.L., Coulson A.R., Fiddes J.C.,
RA   Hutchison C.A. III, Slocombe P.M., Smith M.;
RT   "Nucleotide sequence of bacteriophage phi X174 DNA.";
RL   Nature 265:687-695(1977).
RN   [2]
RP   SEQUENCE REVISION.
RX   PubMed=731693; DOI=10.1016/0022-2836(78)90346-7;
RA   Sanger F., Coulson A.R., Friedmann T., Air G.M., Barrell B.G., Brown N.L.,
RA   Fiddes J.C., Hutchison C.A. III, Slocombe P.M., Smith M.;
RT   "The nucleotide sequence of bacteriophage phiX174.";
RL   J. Mol. Biol. 125:225-246(1978).
RN   [3]
RP   FUNCTION, AND BINDING TO RECEPTOR LIPOPOLYSACCHARIDES.
RX   PubMed=10739948; DOI=10.1093/oxfordjournals.jbchem.a022643;
RA   Inagaki M., Tanaka A., Suzuki R., Wakashima H., Kawaura T., Karita S.,
RA   Nishikawa S., Kashimura N.;
RT   "Characterization of the binding of spike H protein of bacteriophage
RT   phiX174 with receptor lipopolysaccharides.";
RL   J. Biochem. 127:577-583(2000).
RN   [4]
RP   FUNCTION.
RX   PubMed=16143459; DOI=10.1016/j.femsle.2005.08.014;
RA   Inagaki M., Wakashima H., Kato M., Kaitani K., Nishikawa S.;
RT   "Crucial role of the lipid part of lipopolysaccharide for conformational
RT   change of minor spike H protein of bacteriophage phiX174.";
RL   FEMS Microbiol. Lett. 251:305-311(2005).
RN   [5]
RP   CRYSTALLIZATION.
RX   PubMed=1370343; DOI=10.1038/355137a0;
RA   McKenna R., Xia D., Williangmann P., Ilag L.L., Krishnaswamy S.,
RA   Rossmann M.G., Olson N.H., Baker T.S., Incardona N.L.;
RT   "Atomic structure of single-stranded DNA bacteriophage phi X174 and its
RT   functional implications.";
RL   Nature 355:137-143(1992).
RN   [6]
RP   X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX   PubMed=8158636; DOI=10.1006/jmbi.1994.1253;
RA   McKenna R., Ilag L.L., Rossmann M.G.;
RT   "Analysis of the single-stranded DNA bacteriophage phi X174, refined at a
RT   resolution of 3.0 A.";
RL   J. Mol. Biol. 237:517-543(1994).
RN   [7]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 143-221, AND FUNCTION.
RX   PubMed=24336205; DOI=10.1038/nature12816;
RA   Sun L., Young L.N., Zhang X., Boudko S.P., Fokine A., Zbornik E.,
RA   Roznowski A.P., Molineux I.J., Rossmann M.G., Fane B.A.;
RT   "Icosahedral bacteriophage PhiX174 forms a tail for DNA transport during
RT   infection.";
RL   Nature 505:432-435(2014).
CC   -!- FUNCTION: Self-assembles within the capsid. Upon host cell recognition,
CC       probably forms a tube that serves to deliver DNA genome to the host
CC       cytoplasm. This tube protrudes only at the time of infection.
CC       {ECO:0000269|PubMed:10739948, ECO:0000269|PubMed:16143459,
CC       ECO:0000269|PubMed:24336205}.
CC   -!- SUBUNIT: Interacts with B, G and F pentamers to form 12S pre-assembly
CC       complex. Joining of twelve 12S complex form the procapsid.
CC   -!- INTERACTION:
CC       P03646; P03646: H; NbExp=3; IntAct=EBI-16086070, EBI-16086070;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the microviridae H protein family.
CC       {ECO:0000305}.
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DR   EMBL; J02482; AAA32580.1; -; Genomic_DNA.
DR   PIR; D93185; ZHBPF4.
DR   PDB; 4JPN; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J=143-221.
DR   PDB; 4JPP; X-ray; 2.40 A; A/B/C/D/E=143-282.
DR   PDBsum; 4JPN; -.
DR   PDBsum; 4JPP; -.
DR   SMR; P03646; -.
DR   DIP; DIP-60692N; -.
DR   TCDB; 1.K.3.1.1; the phix174 tube-forming spike protein h (phix174-h) family.
DR   Proteomes; UP000005893; Genome.
DR   GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0039638; P:lipopolysaccharide-mediated virion attachment to host cell; IMP:CACAO.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR006777; Microvir_H.
DR   Pfam; PF04687; Microvir_H; 1.
DR   PIRSF; PIRSF004160; Microvir_H; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Capsid protein; Host-virus interaction; Reference proteome;
KW   Viral genome ejection through host cell envelope;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   CHAIN           1..328
FT                   /note="Minor spike protein H"
FT                   /id="PRO_0000164901"
FT   HELIX           146..215
FT                   /evidence="ECO:0007829|PDB:4JPN"
SQ   SEQUENCE   328 AA;  34419 MW;  3793DD830678927C CRC64;
     MFGAIAGGIA SALAGGAMSK LFGGGQKAAS GGIQGDVLAT DNNTVGMGDA GIKSAIQGSN
     VPNPDEAAPS FVSGAMAKAG KGLLEGTLQA GTSAVSDKLL DLVGLGGKSA ADKGKDTRDY
     LAAAFPELNA WERAGADASS AGMVDAGFEN QKELTKMQLD NQKEIAEMQN ETQKEIAGIQ
     SATSRQNTKD QVYAQNEMLA YQQKESTARV ASIMENTNLS KQQQVSEIMR QMLTQAQTAG
     QYFTNDQIKE MTRKVSAEVD LVHQQTQNQR YGSSHIGATA KDISNVVTDA ASGVVDIFHG
     IDKAVADTWN NFWKDGKADG IGSNLSRK