PORP_PSEAE
ID PORP_PSEAE Reviewed; 440 AA.
AC P05695;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Porin P;
DE AltName: Full=Outer membrane protein D1;
DE Flags: Precursor;
GN Name=oprP; OrderedLocusNames=PA3279;
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=ATCC 15692 / PAO1 / H103;
RX PubMed=1697017; DOI=10.1111/j.1365-2958.1990.tb00653.x;
RA Siehnel R.J., Martin N.L., Hancock R.E.W.;
RT "Sequence and relatedness in other bacteria of the Pseudomonas aeruginosa
RT oprP gene coding for the phosphate-specific porin P.";
RL Mol. Microbiol. 4:831-838(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15692 / PAO1 / H103;
RX PubMed=1406271; DOI=10.1111/j.1365-2958.1992.tb01407.x;
RA Siehnel R.J., Egli C., Hancock R.E.W.;
RT "Polyphosphate-selective porin OprO of Pseudomonas aeruginosa: expression,
RT purification and sequence.";
RL Mol. Microbiol. 6:2319-2326(1992).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-56.
RX PubMed=2456446; DOI=10.1111/j.1365-2958.1988.tb00038.x;
RA Siehnel R.J., Worobec E.A., Hancock R.E.W.;
RT "Regulation of components of the Pseudomonas aeruginosa phosphate-
RT starvation-inducible regulon in Escherichia coli.";
RL Mol. Microbiol. 2:347-352(1988).
RN [5]
RP PROTEIN SEQUENCE OF 30-65.
RX PubMed=2451538; DOI=10.1016/0005-2736(88)90082-x;
RA Worobec E.A., Martin N.L., McCubbin W.D., Kay C.M., Brayer G.D.,
RA Hancock R.E.W.;
RT "Large-scale purification and biochemical characterization of
RT crystallization-grade porin protein P from Pseudomonas aeruginosa.";
RL Biochim. Biophys. Acta 939:366-374(1988).
RN [6]
RP CHARACTERIZATION.
RX PubMed=3017428; DOI=10.1016/0005-2736(86)90569-9;
RA Hancock R.E.W., Benz R.;
RT "Demonstration and chemical modification of a specific phosphate binding
RT site in the phosphate-starvation-inducible outer membrane porin protein P
RT of Pseudomonas aeruginosa.";
RL Biochim. Biophys. Acta 860:699-707(1986).
CC -!- FUNCTION: Anion specific, the binding site has higher affinity for
CC phosphate than chloride ions. Porin O has a higher affinity for
CC polyphosphates (tripolyphosphate and pyrophosphate) while porin P has a
CC higher affinity for orthophosphate.
CC -!- SUBUNIT: Homotrimer. Trimer pore size is 0.6 nM.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the OprO/OprP family. {ECO:0000305}.
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DR EMBL; X53313; CAA37395.1; -; Genomic_DNA.
DR EMBL; M86648; AAA25913.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG06667.1; -; Genomic_DNA.
DR EMBL; Y00553; CAA68631.1; -; Genomic_DNA.
DR PIR; F83235; F83235.
DR PIR; S11793; S11793.
DR RefSeq; NP_251969.1; NC_002516.2.
DR RefSeq; WP_003119678.1; NZ_QZGE01000019.1.
DR PDB; 2O4V; X-ray; 1.94 A; A/B/C=30-440.
DR PDBsum; 2O4V; -.
DR AlphaFoldDB; P05695; -.
DR SMR; P05695; -.
DR DIP; DIP-29262N; -.
DR STRING; 287.DR97_4651; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR TCDB; 1.B.5.1.1; the pseudomonas oprp porin (pop) family.
DR PaxDb; P05695; -.
DR PRIDE; P05695; -.
DR EnsemblBacteria; AAG06667; AAG06667; PA3279.
DR GeneID; 882442; -.
DR KEGG; pae:PA3279; -.
DR PATRIC; fig|208964.12.peg.3428; -.
DR PseudoCAP; PA3279; -.
DR HOGENOM; CLU_031025_4_1_6; -.
DR InParanoid; P05695; -.
DR OMA; FRWGVSA; -.
DR PhylomeDB; P05695; -.
DR BioCyc; PAER208964:G1FZ6-3340-MON; -.
DR EvolutionaryTrace; P05695; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IEA:UniProtKB-KW.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR010870; Porin_O/P.
DR Pfam; PF07396; Porin_O_P; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Chloride; Direct protein sequencing;
KW Ion transport; Membrane; Porin; Reference proteome; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2451538"
FT CHAIN 30..440
FT /note="Porin P"
FT /id="PRO_0000025212"
FT CONFLICT 208
FT /note="S -> T (in Ref. 1; CAA37395/AAA25913)"
FT /evidence="ECO:0000305"
FT CONFLICT 394..395
FT /note="HT -> RA (in Ref. 1; CAA37395/AAA25913)"
FT /evidence="ECO:0000305"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 57..73
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 76..80
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 82..98
FT /evidence="ECO:0007829|PDB:2O4V"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:2O4V"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 122..129
FT /evidence="ECO:0007829|PDB:2O4V"
FT TURN 131..134
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 135..141
FT /evidence="ECO:0007829|PDB:2O4V"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:2O4V"
FT TURN 154..156
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 158..161
FT /evidence="ECO:0007829|PDB:2O4V"
FT HELIX 164..168
FT /evidence="ECO:0007829|PDB:2O4V"
FT HELIX 170..173
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 176..186
FT /evidence="ECO:0007829|PDB:2O4V"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 190..203
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 208..223
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 226..238
FT /evidence="ECO:0007829|PDB:2O4V"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 260..262
FT /evidence="ECO:0007829|PDB:2O4V"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 283..298
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 301..314
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 321..333
FT /evidence="ECO:0007829|PDB:2O4V"
FT TURN 343..346
FT /evidence="ECO:0007829|PDB:2O4V"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 360..374
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 389..401
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 403..420
FT /evidence="ECO:0007829|PDB:2O4V"
FT STRAND 428..440
FT /evidence="ECO:0007829|PDB:2O4V"
SQ SEQUENCE 440 AA; 48211 MW; 840243D11CDC7C26 CRC64;
MIRRHSCKGV GSSVAWSLLG LAISAQSLAG TVTTDGADIV IKTKGGLEVA TTDKEFSFKL
GGRLQADYGR FDGYYTNNGN TADAAYFRRA YLEFGGTAYR DWKYQINYDL SRNVGNDSAG
YFDEASVTYT GFNPVNLKFG RFYTDFGLEK ATSSKWVTAL ERNLTYDIAD WVNDNVGTGI
QASSVVGGMA FLSGSVFSEN NNDTDGDSVK RYNLRGVFAP LHEPGNVVHL GLQYAYRDLE
DSAVDTRIRP RMGMRGVSTN GGNDAGSNGN RGLFGGSSAV EGLWKDDSVW GLEGAWALGA
FSAQAEYLRR TVKAERDRED LKASGYYAQL AYTLTGEPRL YKLDGAKFDT IKPENKEIGA
WELFYRYDSI KVEDDNIVVD SATREVGDAK GKTHTLGVNW YANEAVKVSA NYVKAKTDKI
SNANGDDSGD GLVMRLQYVF
