ID   FIB12_BPB03             Reviewed;         860 AA.
AC   Q37893;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Pre-neck appendage protein;
DE   AltName: Full=Gene product 12;
DE            Short=gp12;
DE   AltName: Full=Late protein GP12;
DE   AltName: Full=NP1;
DE   AltName: Full=Protein p12;
GN   Name=12;
OS   Bacillus phage B103 (Bacteriophage B103).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Picovirinae; Beecentumtrevirus.
OX   NCBI_TaxID=10778;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=9358052; DOI=10.1016/s0378-1119(97)00363-6;
RA   Pecenkova T., Benes V., Paces J., Vlcek C., Paces V.;
RT   "Bacteriophage B103: complete DNA sequence of its genome and relationship
RT   to other Bacillus phages.";
RL   Gene 199:157-163(1997).
CC   -!- FUNCTION: Structural component of the 12 appendages that hang from the
CC       lower collar. Adhesion protein that binds to the host cell surface
CC       during virus attachment and mediates teichoic acids degradation.
CC       {ECO:0000250|UniProtKB:P20345}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P20345};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P20345};
CC   -!- SUBUNIT: Homotrimer. Each appendage is a homotrimer of gp12*.
CC       {ECO:0000250|UniProtKB:P20345}.
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P20345}.
CC       Note=Present in 36 copies in the virion.
CC       {ECO:0000250|UniProtKB:P20345}.
CC   -!- DOMAIN: The N-terminus has three domains that function to attach the
CC       appendages to the phage, digest the cell wall teichoic acids, and bind
CC       irreversibly to the host. The C-terminus is an autochaperone that aids
CC       trimerization. {ECO:0000250|UniProtKB:P20345}.
CC   -!- PTM: Autocleaved to produce the 74 kDa gp12* assembly attached to the
CC       phage particles. Autocleavage of the C-terminus is a posttrimerization
CC       event that is followed by an ATP-dependent release.
CC       {ECO:0000250|UniProtKB:P20345}.
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DR   EMBL; X99260; CAA67660.1; -; Genomic_DNA.
DR   RefSeq; NP_690646.1; NC_004165.1.
DR   SMR; Q37893; -.
DR   MEROPS; G02.001; -.
DR   GeneID; 955361; -.
DR   KEGG; vg:955361; -.
DR   Proteomes; UP000000971; Genome.
DR   GO; GO:0098024; C:virus tail, fiber; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0098671; P:adhesion receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR   GO; GO:0098994; P:disruption of host cell envelope during viral entry; IEA:UniProtKB-KW.
DR   Gene3D; 2.160.20.10; -; 1.
DR   InterPro; IPR006626; PbH1.
DR   InterPro; IPR024535; Pectate_lyase_SF_prot.
DR   InterPro; IPR012334; Pectin_lyas_fold.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   InterPro; IPR021865; Peptidase_G2.
DR   Pfam; PF12708; Pectate_lyase_3; 1.
DR   Pfam; PF11962; Peptidase_G2; 1.
DR   SMART; SM00710; PbH1; 8.
DR   SUPFAM; SSF51126; SSF51126; 1.
PE   3: Inferred from homology;
KW   ATP-binding;
KW   Degradation of host cell envelope components during virus entry;
KW   Host-virus interaction; Late protein; Magnesium; Metal-binding;
KW   Nucleotide-binding; Repeat; Viral attachment to host adhesion receptor;
KW   Viral attachment to host cell; Viral tail fiber protein;
KW   Viral tail protein; Virion; Virus entry into host cell.
FT   CHAIN           1..860
FT                   /note="Pre-neck appendage protein"
FT                   /id="PRO_0000106591"
FT   ACT_SITE        701
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:P20345"
FT   BINDING         309
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P20345"
FT   BINDING         311
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250|UniProtKB:P20345"
FT   BINDING         752..801
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:P20345"
FT   SITE            697..698
FT                   /note="Cleavage"
FT                   /evidence="ECO:0000250|UniProtKB:P20345"
SQ   SEQUENCE   860 AA;  91742 MW;  AC5B38F4BC65ECB0 CRC64;
     MQKPELRRFE KLGEMMVQVY ERYLPTAFDE SMTLLEKMNK IIEYLNQIGR LTNDVVEEWN
     KVMEWILNDG LEDYVKETLE KWYEEGKFAD LVIQVIDELK QFGVSVKTYG AVGDGKTDDI
     EAFEKAIASG YPVYIPNGKF AVSRSIKIPS NTVITGAGID NAVVTFLDSV PLGDSLMIND
     NYATGNENIY LSDFTLDGNC QRFGVNAIGS GGSRDSNLSI HASKNVHINR IKSINATLHG
     IDITCGGLDY PYMGDGTTAP YPSRDIYISD CEAPSLGDDG ITTNNSEYIT ISNCNCHDPR
     LLNNCNGIEI DDGSRHVQLS NNISKNCFGG VEVKAHGNVP AAYNVSINGH MSIGDVRSYN
     FRHIGHHSAT DPESMSAKNI ICNNLMSVNP NNKRGFQNNA APRVLAVSAY YGVVVNGLSA
     YTTEPANLTE TAISVQFRAR NVSLSGIVMT GFSMAENAIY VIGGSRGGDS VNISNVTLNN
     SGRNGVAIGS GIDNVSISNV SAIGDGIANP IAIVKTVNSN PQISGVNGIG YPTVCQVAGV
     AYNDGLTLFN GAFRGATSSS EFIHSEGFVL GSTSKSGATA SKSGVVSSSN SIAKAERSLI
     AGSASCTTSG SYNTILSSLN CETTDTGNLI STSSASKATG NRNIILASYG VLASGSYKVN
     GGYGGEGTPS ASNIKLGNSL NGHIKAKNTV TGANTWSDYG EYFESVDGQA IETGYLVTLE
     GSKIRKAQEG EKIIGAISET AGIILGESTW NWQGQYLKNE FGGLIYETVE IDEGVFEKMP
     KINPSYNPKL EYLSRGERPE WNIVGLIGQI MVRIDDTVKI GSGISAKDGI ATDGDTGIVM
     QITTPYESSK GYGVAKVLLK