位置:首页 > 蛋白库 > FIB12_BPPZA
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024