PYS2_PSEAE
ID PYS2_PSEAE Reviewed; 689 AA.
AC Q06584;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Pyocin-S2;
DE EC=3.1.-.-;
DE AltName: Full=Killer protein;
GN Name=pys2; OrderedLocusNames=PA1150;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-18.
RC STRAIN=PAO;
RX PubMed=8491711; DOI=10.1128/jb.175.10.2907-2916.1993;
RA Sano Y., Matsui H., Kobayashi M., Kageyama M.;
RT "Molecular structures and functions of pyocins S1 and S2 in Pseudomonas
RT aeruginosa.";
RL J. Bacteriol. 175:2907-2916(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Causes breakdown of chromosomal DNA as well as complete
CC inhibition of lipid synthesis in sensitive cells.
CC -!- SUBUNIT: Purified pyocin S2 makes up a complex of the two (large and
CC small) proteins. The large protein, but not the pyocin complex, shows
CC in vitro DNase activity.
CC -!- MISCELLANEOUS: Pyocins contain N-terminal receptor-binding domain,
CC translocation domain and C-terminal DNase domain.
CC -!- SIMILARITY: Belongs to the colicin/pyosin nuclease family.
CC {ECO:0000305}.
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; D12708; BAA02203.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04539.1; -; Genomic_DNA.
DR PIR; C36907; C36907.
DR PIR; D83501; D83501.
DR RefSeq; NP_249841.1; NC_002516.2.
DR RefSeq; WP_003112476.1; NC_002516.2.
DR PDB; 4QKO; X-ray; 1.80 A; B/D/F/H=556-689.
DR PDB; 5ODW; X-ray; 2.80 A; C/D=1-209.
DR PDBsum; 4QKO; -.
DR PDBsum; 5ODW; -.
DR AlphaFoldDB; Q06584; -.
DR SMR; Q06584; -.
DR STRING; 208964.PA1150; -.
DR TCDB; 1.C.1.4.2; the channel-forming colicin (colicin) family.
DR PaxDb; Q06584; -.
DR PRIDE; Q06584; -.
DR EnsemblBacteria; AAG04539; AAG04539; PA1150.
DR GeneID; 878080; -.
DR KEGG; pae:PA1150; -.
DR PATRIC; fig|208964.12.peg.1196; -.
DR PseudoCAP; PA1150; -.
DR HOGENOM; CLU_458468_0_0_6; -.
DR OMA; NTYAMPA; -.
DR PhylomeDB; Q06584; -.
DR BioCyc; PAER208964:G1FZ6-1176-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0005102; F:signaling receptor binding; IEA:InterPro.
DR GO; GO:0019835; P:cytolysis; IDA:PseudoCAP.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR CDD; cd00085; HNHc; 1.
DR Gene3D; 3.90.540.10; -; 1.
DR InterPro; IPR037146; Colicin/pyocin_DNase_dom_sf.
DR InterPro; IPR044925; His-Me_finger_sf.
DR InterPro; IPR003615; HNH_nuc.
DR InterPro; IPR003060; Pyocin_killer.
DR InterPro; IPR016128; Pyosin/cloacin_T_dom.
DR InterPro; IPR036302; Pyosin/cloacin_T_dom_sf.
DR Pfam; PF06958; Pyocin_S; 1.
DR PRINTS; PR01300; PYOCINKILLER.
DR SMART; SM00507; HNHc; 1.
DR SUPFAM; SSF54060; SSF54060; 1.
DR SUPFAM; SSF69369; SSF69369; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic; Antimicrobial; Bacteriocin;
KW Direct protein sequencing; Endonuclease; Hydrolase; Metal-binding;
KW Nuclease; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8491711"
FT CHAIN 2..689
FT /note="Pyocin-S2"
FT /id="PRO_0000218686"
FT BINDING 656
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 681
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 685
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT CONFLICT 605
FT /note="R -> RR (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:5ODW"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:5ODW"
FT HELIX 47..70
FT /evidence="ECO:0007829|PDB:5ODW"
FT HELIX 72..86
FT /evidence="ECO:0007829|PDB:5ODW"
FT HELIX 96..121
FT /evidence="ECO:0007829|PDB:5ODW"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:5ODW"
FT HELIX 133..148
FT /evidence="ECO:0007829|PDB:5ODW"
FT HELIX 153..204
FT /evidence="ECO:0007829|PDB:5ODW"
FT HELIX 576..581
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 590..596
FT /evidence="ECO:0007829|PDB:4QKO"
FT STRAND 600..603
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 604..617
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 621..624
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 627..633
FT /evidence="ECO:0007829|PDB:4QKO"
FT TURN 634..636
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 643..645
FT /evidence="ECO:0007829|PDB:4QKO"
FT STRAND 654..659
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 661..663
FT /evidence="ECO:0007829|PDB:4QKO"
FT STRAND 667..669
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 670..672
FT /evidence="ECO:0007829|PDB:4QKO"
FT STRAND 673..676
FT /evidence="ECO:0007829|PDB:4QKO"
FT HELIX 678..685
FT /evidence="ECO:0007829|PDB:4QKO"
SQ SEQUENCE 689 AA; 73854 MW; 3235FAB8592D0EF0 CRC64;
MAVNDYEPGS MVITHVQGGG RDIIQYIPAR SSYGTPPFVP PGPSPYVGTG MQEYRKLRST
LDKSHSELKK NLKNETLKEV DELKSEAGLP GKAVSANDIR DEKSIVDALM DAKAKSLKAI
EDRPANLYTA SDFPQKSESM YQSQLLASRK FYGEFLDRHM SELAKAYSAD IYKAQIAILK
QTSQELENKA RSLEAEAQRA AAEVEADYKA RKANVEKKVQ SELDQAGNAL PQLTNPTPEQ
WLERATQLVT QAIANKKKLQ TANNALIAKA PNALEKQKAT YNADLLVDEI ASLQARLDKL
NAETARRKEI ARQAAIRAAN TYAMPANGSV VATAAGRGLI QVAQGAASLA QAISDAIAVL
GRVLASAPSV MAVGFASLTY SSRTAEQWQD QTPDSVRYAL GMDAAKLGLP PSVNLNAVAK
ASGTVDLPMR LTNEARGNTT TLSVVSTDGV SVPKAVPVRM AAYNATTGLY EVTVPSTTAE
APPLILTWTP ASPPGNQNPS STTPVVPKPV PVYEGATLTP VKATPETYPG VITLPEDLII
GFPADSGIKP IYVMFRDPRD VPGAATGKGQ PVSGNWLGAA SQGEGAPIPS QIADKLRGKT
FKNWRDFREQ FWIAVANDPE LSKQFNPGSL AVMRDGGAPY VRESEQAGGR IKIEIHHKVR
IADGGGVYNM GNLVAVTPKR HIEIHKGGK
