FIB12_BPPH2
ID FIB12_BPPH2 Reviewed; 854 AA.
AC P20345; B3VMP8;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Pre-neck appendage protein {ECO:0000305};
DE AltName: Full=Gene product 12 {ECO:0000305};
DE Short=gp12 {ECO:0000305};
DE AltName: Full=NP1 {ECO:0000303|PubMed:7241648};
DE AltName: Full=Protein p12 {ECO:0000305};
DE Contains:
DE RecName: Full=gp12*;
GN Name=12;
OS Bacillus phage phi29 (Bacteriophage phi-29).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Salasmaviridae; Picovirinae; Salasvirus.
OX NCBI_TaxID=10756;
OH NCBI_TaxID=1423; Bacillus subtilis.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3803926; DOI=10.1016/0378-1119(86)90406-3;
RA Vlcek C., Paces V.;
RT "Nucleotide sequence of the late region of Bacillus phage phi 29 completes
RT the 19,285-bp sequence of phi 29 genome. Comparison with the homologous
RT sequence of phage PZA.";
RL Gene 46:215-225(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=7241648; DOI=10.1128/jvi.38.1.15-19.1981;
RA Villanueva N., Salas M.;
RT "Adsorption of bacteriophage phi 29 to Bacillus subtilis through the neck
RT appendages of the viral particle.";
RL J. Virol. 38:15-19(1981).
RN [4]
RP SUBCELLULAR LOCATION.
RX PubMed=11562162; DOI=10.1006/jsbi.2001.4375;
RA Peterson C., Simon M., Hodges J., Mertens P., Higgins L., Egelman E.,
RA Anderson D.;
RT "Composition and mass of the bacteriophage phi29 prohead and virion.";
RL J. Struct. Biol. 135:18-25(2001).
RN [5] {ECO:0007744|PDB:3GQ7, ECO:0007744|PDB:3GQ8, ECO:0007744|PDB:3GQ9, ECO:0007744|PDB:3GQA, ECO:0007744|PDB:3GQH, ECO:0007744|PDB:3GQK, ECO:0007744|PDB:3SUC}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 692-854 IN COMPLEX WITH ATP AND
RP MAGNESIUM, SUBUNIT, CLEAVAGE, DOMAIN, MUTAGENESIS OF GLU-695, ACTIVE SITE,
RP SUBCELLULAR LOCATION, AND COFACTOR.
RX PubMed=19450535; DOI=10.1016/j.molcel.2009.04.009;
RA Xiang Y., Leiman P.G., Li L., Grimes S., Anderson D.L., Rossmann M.G.;
RT "Crystallographic insights into the autocatalytic assembly mechanism of a
RT bacteriophage tail spike.";
RL Mol. Cell 34:375-386(2009).
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:0000269|PubMed:7241648}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19450535};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:19450535};
CC -!- SUBUNIT: Homotrimer. Each appendage is a homotrimer of gp12*.
CC {ECO:0000269|PubMed:19450535}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:11562162,
CC ECO:0000269|PubMed:19450535}. Note=Present in 36 copies in the virion.
CC {ECO:0000305|PubMed:19450535}.
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:0000269|PubMed:19450535}.
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:0000269|PubMed:19450535}.
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DR EMBL; M14782; AAA32285.1; -; Genomic_DNA.
DR EMBL; EU771092; ACE96035.1; -; Genomic_DNA.
DR PIR; G25816; WMBP22.
DR RefSeq; YP_002004541.1; NC_011048.1.
DR PDB; 3GQ7; X-ray; 2.05 A; A=89-691.
DR PDB; 3GQ8; X-ray; 2.00 A; A=89-691.
DR PDB; 3GQ9; X-ray; 2.00 A; A=89-691.
DR PDB; 3GQA; X-ray; 2.10 A; A=89-691.
DR PDB; 3GQH; X-ray; 1.80 A; A/B/C=692-854.
DR PDB; 3GQK; X-ray; 2.50 A; A=692-854.
DR PDB; 3SUC; X-ray; 2.15 A; A=89-854.
DR PDB; 6QZ9; EM; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-854.
DR PDB; 6QZF; EM; 3.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X/Y/Z/a/b/c/d=1-854.
DR PDBsum; 3GQ7; -.
DR PDBsum; 3GQ8; -.
DR PDBsum; 3GQ9; -.
DR PDBsum; 3GQA; -.
DR PDBsum; 3GQH; -.
DR PDBsum; 3GQK; -.
DR PDBsum; 3SUC; -.
DR PDBsum; 6QZ9; -.
DR PDBsum; 6QZF; -.
DR SMR; P20345; -.
DR MEROPS; G02.001; -.
DR GeneID; 6446499; -.
DR KEGG; vg:6446499; -.
DR EvolutionaryTrace; P20345; -.
DR Proteomes; UP000001207; 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 GO; GO:0019062; P:virion attachment to host cell; IDA:UniProtKB.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding;
KW Degradation of host cell envelope components during virus entry;
KW Host-virus interaction; Late protein; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Repeat;
KW Viral attachment to host adhesion receptor; Viral attachment to host cell;
KW Viral tail fiber protein; Viral tail protein; Virion;
KW Virus entry into host cell.
FT CHAIN 1..854
FT /note="Pre-neck appendage protein"
FT /id="PRO_0000106592"
FT CHAIN 1..691
FT /note="gp12*"
FT /id="PRO_0000432876"
FT ACT_SITE 695
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:19450535"
FT BINDING 285
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19450535,
FT ECO:0007744|PDB:3SUC"
FT BINDING 310
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19450535,
FT ECO:0007744|PDB:3SUC"
FT BINDING 312
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000269|PubMed:19450535,
FT ECO:0007744|PDB:3SUC"
FT BINDING 746..795
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0007744|PDB:3GQK, ECO:0007744|PDB:3SUC"
FT SITE 691..692
FT /note="Cleavage"
FT /evidence="ECO:0000269|PubMed:19450535"
FT MUTAGEN 695
FT /note="E->Q: Complete loss of autocleavage. No effect on
FT trimerization or enzymatic teichoic acid degrading
FT activity."
FT /evidence="ECO:0000269|PubMed:19450535"
FT CONFLICT 181
FT /note="Q -> E (in Ref. 2; ACE96035)"
FT /evidence="ECO:0000305"
FT CONFLICT 372
FT /note="D -> A (in Ref. 2; ACE96035)"
FT /evidence="ECO:0000305"
FT CONFLICT 449
FT /note="G -> V (in Ref. 2; ACE96035)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="D -> E (in Ref. 2; ACE96035)"
FT /evidence="ECO:0000305"
FT CONFLICT 535
FT /note="A -> V (in Ref. 2; ACE96035)"
FT /evidence="ECO:0000305"
FT CONFLICT 627
FT /note="Q -> K (in Ref. 2; ACE96035)"
FT /evidence="ECO:0000305"
FT CONFLICT 777
FT /note="S -> N (in Ref. 2; ACE96035)"
FT /evidence="ECO:0000305"
FT HELIX 89..100
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:3GQ8"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:3GQ8"
FT HELIX 121..129
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 134..136
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 147..149
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 151..158
FT /evidence="ECO:0007829|PDB:3GQ8"
FT TURN 160..162
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 163..167
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:3GQ8"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 188..198
FT /evidence="ECO:0007829|PDB:3GQ8"
FT HELIX 201..204
FT /evidence="ECO:0007829|PDB:3GQ8"
FT TURN 213..216
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 225..236
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 241..245
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 247..250
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 265..271
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 273..276
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 288..294
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3GQ9"
FT STRAND 308..311
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 316..336
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 344..355
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 369..372
FT /evidence="ECO:0007829|PDB:3SUC"
FT STRAND 379..390
FT /evidence="ECO:0007829|PDB:3GQ8"
FT HELIX 397..400
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 404..410
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 412..422
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 441..452
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 457..462
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 472..481
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 484..489
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 496..504
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 513..520
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 541..543
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 561..564
FT /evidence="ECO:0007829|PDB:3SUC"
FT STRAND 568..572
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 574..579
FT /evidence="ECO:0007829|PDB:3SUC"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 597..603
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 611..618
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 620..624
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 630..639
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 645..651
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 659..672
FT /evidence="ECO:0007829|PDB:3GQ8"
FT TURN 673..676
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 677..682
FT /evidence="ECO:0007829|PDB:3GQ8"
FT STRAND 693..699
FT /evidence="ECO:0007829|PDB:3GQH"
FT HELIX 700..702
FT /evidence="ECO:0007829|PDB:3SUC"
FT STRAND 710..714
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 723..725
FT /evidence="ECO:0007829|PDB:3GQK"
FT STRAND 729..731
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 736..739
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 748..750
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 760..764
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 766..768
FT /evidence="ECO:0007829|PDB:3SUC"
FT STRAND 770..774
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:3GQH"
FT HELIX 789..791
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 795..808
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 816..821
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 824..838
FT /evidence="ECO:0007829|PDB:3GQH"
FT TURN 842..844
FT /evidence="ECO:0007829|PDB:3GQH"
FT STRAND 847..853
FT /evidence="ECO:0007829|PDB:3GQH"
SQ SEQUENCE 854 AA; 92103 MW; 373D4F4275D73EED CRC64;
MSTKPELKRF EQFGEMMVQL YERYLPTAFD ESLTLLEKMN KIIHYLNEIG KVTNELIEEW
NKVMEWILND GLEDLVKETL ERWYEEGKFA DLVIQVIDEL KQFGVSVKTY GAKGDGVTDD
IRAFEKAIES GFPVYVPYGT FMVSRGIKLP SNTVLTGAGK RNAVIKFMDS VGRGESLMYN
QNVTTGNENI FLSSFTLDGN NKRLGQGISG IGGSRESNLS IRACHNVYIR DIEAVDCTLH
GIDITCGGLD YPYLGDGTTA PNPSENIWIE NCEATGFGDD GITTHHSQYI NILNCYSHDP
RLTANCNGFE IDDGSRHVVL SNNRSKGCYG GIEIKAHGDA PAAYNISING HMSVEDVRSY
NFRHIGHHAA TDPQSVSAKN IVASNLVSIR PNNKRGFQDN ATPRVLAVSA YYGVVINGLT
GYTDDPNLLT ETVVSVQFRA RNCSLNGVGL TGFSNSDNGI YVIGGSRGGD AVNISNVTLN
NSGRYGVSIG SGIENVSITN ISGIGDGINS PVALVSTINS NPEISGLSSI GYPTAARVAG
TDYNDGLTLF NGAFRASTTS SGKIHSEGFI MGSTSGCEAS VSKSGVLTSS SSKTSSERSL
IAGSSTSEAK GTYNTILGSL GAVADEQFAA LISASQSRAS GNHNLILSSY GINTTGSYKV
NGGFEKINWE LDSLNGRIKA RDTVTGGNTW SDFAEYFESL DGQVIETGYL VTLEKGKIRK
AEKGEKIIGV ISETAGFVLG ESSFEWQGAV LKNEFGGIIY EEVTTEDGVK FKRPLPSPDF
DPNKNYIPRS QRREWHVVGL LGQIAVRIDE TVKQGHGIDA VGGVATDGDN FIVQEITTPY
TKEKGYGVAI VLVK
