FIB12_BPB03
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