FIB12_BPPZA
ID FIB12_BPPZA Reviewed; 854 AA.
AC P07537;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Preneck appendage protein {ECO:0000250|UniProtKB:P20345};
DE AltName: Full=Gene product 12 {ECO:0000250|UniProtKB:P20345};
DE Short=gp12 {ECO:0000250|UniProtKB:P20345};
DE AltName: Full=Protein p12 {ECO:0000250|UniProtKB:P20345};
DE Contains:
DE RecName: Full=gp12* {ECO:0000250|UniProtKB:P20345};
GN Name=12;
OS Bacillus phage PZA (Bacteriophage PZA).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus; Bacillus virus PZA.
OX NCBI_TaxID=10757;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3095188; DOI=10.1016/0378-1119(86)90048-x;
RA Paces V., Vlcek C., Urbanek P.;
RT "Nucleotide sequence of the late region of Bacillus subtilis phage PZA, a
RT close relative of phi 29.";
RL Gene 44:107-114(1986).
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; M11813; AAA88489.1; -; Genomic_DNA.
DR PIR; G24831; WMBP12.
DR SMR; P07537; -.
DR MEROPS; G02.001; -.
DR PRIDE; P07537; -.
DR Proteomes; UP000000855; 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; 6.
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..854
FT /note="Preneck appendage protein"
FT /id="PRO_0000106593"
FT CHAIN 1..691
FT /note="gp12*"
FT /evidence="ECO:0000250|UniProtKB:P20345"
FT /id="PRO_0000436071"
FT ACT_SITE 695
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P20345"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P20345"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P20345"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P20345"
FT BINDING 746..795
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P20345"
FT SITE 691..692
FT /note="Cleavage"
FT /evidence="ECO:0000250|UniProtKB:P20345"
SQ SEQUENCE 854 AA; 92073 MW; 3FB2F23652DB8E3F CRC64;
MSTKPELKRF EQFGEIMVQL YERYLPTAFD ESLTLLEKMN KIIHYLNEIG KVTNELIEEW
NKVMEWILND GLEDLVKETL ERWYEEGKFA DLVIQVIDEL KQFGVSVKTY GAKGDGVTDD
IKAFEKAIES GFPVYVPYGT FMVSRGIKLP SNTVLTGAGK RNAVIKFMDS VGRGESLMYN
ENVTTGNENI FLSSFTLDGN NKRLGQGISG IGGSRESNLS IRACHNVYIR DIEAVDCTLH
GIDITCGGLD YPYLGDGTTA PNPSENIWIE NCEATGFGDD GITTHHSQYI NILNCYSHDP
RLTANCNGFE IDDGSRHVVL SNNRSKGCYG GIEIKAHGDA PAAYNISVNG HMSVEDVRSY
NFRHIGHHAA TDPQSVSAKN IVASNLVSIR PNNKRGFQDN ATPRVLAVSA YYGVVINGLT
GYTDDPNLLT ETVVSVQFRA RNCSLNGVAL TGFSNSENGI YVIGGSRGGD AVNISNVTLN
NSGRYGVSIG SGIENVSITN ISGIGDGINS PVALVSTINS NPEISGLSSI GYPTVARVAG
TDYNDGLTLF NGAFRASTTS SGKIHSEGFI MGSTSGCEAS VSKSGILTSS SSKTSSERSL
IAGSSTSEAT GTYNTILGSL GAVADEQFAG LISASQSRAS GNHNLILSSY GINTVGSYKV
NGGFEKINWE LDSLNGRIKA RDTVTGGNTW SDFAEYFESL DGQVIETGYL VTLDKGKIRK
AEKGEKIIGV ISETAGFVLG ESSFEWQGAV LKNEFGGIVY EEVTTEDGVK FKRPLPNPDF
DPNKNYIPRS QRREWHVVGL LGQIAVRIDD TVKQGQGIDA VGGVATDGNN FIVKEITTPY
NKEKGYGVAI VLIK
