PHZB2_PSEAE
ID PHZB2_PSEAE Reviewed; 162 AA.
AC Q9S508; Q7DCE0;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Phenazine biosynthesis protein PhzB2 {ECO:0000303|PubMed:11591691};
GN Name=phzB2 {ECO:0000303|PubMed:11591691}; OrderedLocusNames=PA1900;
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].
RC STRAIN=UCBPP-PA14;
RX PubMed=9989496; DOI=10.1016/s0092-8674(00)80958-7;
RA Mahajan-Miklos S., Tan M.-W., Rahme L.G., Ausubel F.M.;
RT "Molecular mechanisms of bacterial virulence elucidated using a Pseudomonas
RT aeruginosa-Caenorhabditis elegans pathogenesis model.";
RL Cell 96:47-56(1999).
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).
RN [3]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11591691; DOI=10.1128/jb.183.21.6454-6465.2001;
RA Mavrodi D.V., Bonsall R.F., Delaney S.M., Soule M.J., Phillips G.,
RA Thomashow L.S.;
RT "Functional analysis of genes for biosynthesis of pyocyanin and phenazine-
RT 1-carboxamide from Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 183:6454-6465(2001).
RN [4]
RP FUNCTION, AND INDUCTION.
RX PubMed=23129634; DOI=10.1073/pnas.1213901109;
RA Recinos D.A., Sekedat M.D., Hernandez A., Cohen T.S., Sakhtah H.,
RA Prince A.S., Price-Whelan A., Dietrich L.E.;
RT "Redundant phenazine operons in Pseudomonas aeruginosa exhibit environment-
RT dependent expression and differential roles in pathogenicity.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:19420-19425(2012).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), AND SUBUNIT.
RG Joint center for structural genomics (JCSG);
RT "Crystal structure of protein PhzB2 with cystatin-like fold and unknown
RT function in phenazine biosynthesis (NP_250591.1) from Pseudomonas
RT aeruginosa at 1.90 A resolution.";
RL Submitted (DEC-2008) to the PDB data bank.
CC -!- FUNCTION: Involved in the biosynthesis of the antibiotic phenazine, a
CC nitrogen-containing heterocyclic molecule having important roles in
CC virulence, competition and biological control. PhzB2 (operon
CC phzA2B2C2E2F2G2) has a role in the biosynthesis of the phenazine during
CC both planktonic growth and biofilm development, and in host infection
CC during biofilm development. {ECO:0000269|PubMed:23129634,
CC ECO:0000305|PubMed:11591691}.
CC -!- PATHWAY: Antibiotic biosynthesis; phenazine biosynthesis.
CC {ECO:0000305|PubMed:11591691}.
CC -!- SUBUNIT: Homodimer. {ECO:0000305|Ref.5}.
CC -!- INDUCTION: In liquid cultures (aerobic), phz2 operon is induced by
CC quinolone signal via 2-heptyl-3-hydroxy-4-quinolone (PQS). In biofilm
CC (microaerobic), phz2 operon is induced by quinolone signal via 4-
CC hydroxy-2-heptylquinoline (HHQ), a precursor of PQS.
CC {ECO:0000269|PubMed:23129634}.
CC -!- SIMILARITY: Belongs to the PhzA/PhzB family. {ECO:0000305}.
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DR EMBL; AF092442; AAD45625.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05289.1; -; Genomic_DNA.
DR PIR; F83407; F83407.
DR RefSeq; NP_250591.1; NC_002516.2.
DR RefSeq; WP_003115119.1; NZ_QZGE01000003.1.
DR PDB; 3FF0; X-ray; 1.90 A; A/B=1-162.
DR PDBsum; 3FF0; -.
DR AlphaFoldDB; Q9S508; -.
DR SMR; Q9S508; -.
DR STRING; 287.DR97_5947; -.
DR PaxDb; Q9S508; -.
DR PRIDE; Q9S508; -.
DR DNASU; 878211; -.
DR EnsemblBacteria; AAG05289; AAG05289; PA1900.
DR GeneID; 878211; -.
DR KEGG; pae:PA1900; -.
DR PATRIC; fig|208964.12.peg.1978; -.
DR PseudoCAP; PA1900; -.
DR HOGENOM; CLU_141345_0_0_6; -.
DR OMA; EWYNIQV; -.
DR PhylomeDB; Q9S508; -.
DR BioCyc; PAER208964:G1FZ6-1940-MON; -.
DR UniPathway; UPA00099; -.
DR EvolutionaryTrace; Q9S508; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0002047; P:phenazine biosynthetic process; IDA:PseudoCAP.
DR InterPro; IPR032710; NTF2-like_dom_sf.
DR InterPro; IPR004964; PhzA_PhzB.
DR Pfam; PF03284; PHZA_PHZB; 1.
DR SUPFAM; SSF54427; SSF54427; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic biosynthesis; Reference proteome; Virulence.
FT CHAIN 1..162
FT /note="Phenazine biosynthesis protein PhzB2"
FT /id="PRO_0000287801"
FT HELIX 1..3
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 11..13
FT /evidence="ECO:0007829|PDB:3FF0"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:3FF0"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 42..52
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 54..57
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 59..63
FT /evidence="ECO:0007829|PDB:3FF0"
FT HELIX 64..77
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 82..93
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 115..128
FT /evidence="ECO:0007829|PDB:3FF0"
FT STRAND 131..139
FT /evidence="ECO:0007829|PDB:3FF0"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:3FF0"
SQ SEQUENCE 162 AA; 19028 MW; 5D1A8FE8871AA0FD CRC64;
MLDNAIPQGF EDAVELRRKN RETVVKYMNT KGQDRLRRHE LFVEDGCGGL WTTDTGSPIV
IRGKDKLAEH AVWSLKCFPD WEWYNIKVFE TDDPNHFWVE CDGHGKILFP GYPEGYYENH
FLHSFELDDG KIKRNREFMN VFQQLRALSI PVPQIKREGI PT
