PORD_PSEAE
ID PORD_PSEAE Reviewed; 443 AA.
AC P32722;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Porin D;
DE EC=3.4.21.-;
DE AltName: Full=Imipenem/basic amino acid-specific outer membrane pore;
DE AltName: Full=Outer membrane protein D2;
DE Flags: Precursor;
GN Name=oprD; OrderedLocusNames=PA0958;
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].
RX PubMed=1339257; DOI=10.1128/aac.36.8.1791;
RA Yoneyama H., Yoshihara E., Nakae T.;
RT "Nucleotide sequence of the protein D2 gene of Pseudomonas aeruginosa.";
RL Antimicrob. Agents Chemother. 36:1791-1793(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 24-40.
RC STRAIN=ATCC 15692 / PAO1 / H103;
RX PubMed=1427017; DOI=10.1016/0378-1097(92)90347-q;
RA Huang H., Siehnel R.J., Bellido F., Rawling E., Hancock R.E.W.;
RT "Analysis of two gene regions involved in the expression of the imipenem-
RT specific, outer membrane porin protein OprD of Pseudomonas aeruginosa.";
RL FEMS Microbiol. Lett. 76:267-274(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 PROTEIN SEQUENCE OF 24-48.
RX PubMed=8012497; DOI=10.1159/000468649;
RA Michea-Hamzehpour M., Sanchez J.-C., Epp S.F., Paquet N., Hughes G.J.,
RA Hochstrasser D.F., Pechere J.-C.;
RT "Two-dimensional polyacrylamide gel electrophoresis isolation and
RT microsequencing of Pseudomonas aeruginosa proteins.";
RL Enzyme Protein 47:1-8(1993).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2118530; DOI=10.1016/s0021-9258(18)55452-1;
RA Trias J., Nikaido H.;
RT "Protein D2 channel of the Pseudomonas aeruginosa outer membrane has a
RT binding site for basic amino acids and peptides.";
RL J. Biol. Chem. 265:15680-15684(1990).
RN [6]
RP FUNCTION AS A SERINE PROTEASE.
RX PubMed=8843159; DOI=10.1016/0014-5793(96)00945-3;
RA Yoshihara E., Gotoh N., Nishino T., Nakae T.;
RT "Protein D2 porin of the Pseudomonas aeruginosa outer membrane bears the
RT protease activity.";
RL FEBS Lett. 394:179-182(1996).
RN [7]
RP MUTAGENESIS OF HIS-179; ASP-231; SER-319 AND HIS-390, AND ACTIVE SITES.
RX PubMed=9636669; DOI=10.1006/bbrc.1998.8745;
RA Yoshihara E., Yoneyama H., Ono T., Nakae T.;
RT "Identification of the catalytic triad of the protein D2 protease in
RT Pseudomonas aeruginosa.";
RL Biochem. Biophys. Res. Commun. 247:142-145(1998).
CC -!- FUNCTION: Porin with a specificity for basic amino acids. Also
CC possesses serine protease activity. {ECO:0000269|PubMed:2118530,
CC ECO:0000269|PubMed:8843159}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2118530};
CC Multi-pass membrane protein {ECO:0000269|PubMed:2118530}.
CC -!- SIMILARITY: Belongs to the outer membrane porin (Opr) (TC 1.B.25)
CC family. {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; X63152; CAA44855.1; -; Genomic_DNA.
DR EMBL; Z14065; CAA78448.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG04347.1; -; Genomic_DNA.
DR PIR; S23771; S23771.
DR RefSeq; NP_249649.1; NC_002516.2.
DR RefSeq; WP_003112576.1; NZ_QZGE01000007.1.
DR PDB; 2ODJ; X-ray; 2.90 A; A/B=26-443.
DR PDB; 3SY7; X-ray; 2.15 A; A=24-443.
DR PDB; 4FOZ; X-ray; 2.40 A; A=24-443.
DR PDBsum; 2ODJ; -.
DR PDBsum; 3SY7; -.
DR PDBsum; 4FOZ; -.
DR AlphaFoldDB; P32722; -.
DR SMR; P32722; -.
DR DIP; DIP-29627N; -.
DR STRING; 287.DR97_979; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR TCDB; 1.B.25.1.1; the outer membrane porin (opr) family.
DR PaxDb; P32722; -.
DR PRIDE; P32722; -.
DR EnsemblBacteria; AAG04347; AAG04347; PA0958.
DR GeneID; 881970; -.
DR KEGG; pae:PA0958; -.
DR PATRIC; fig|208964.12.peg.996; -.
DR PseudoCAP; PA0958; -.
DR HOGENOM; CLU_042378_2_0_6; -.
DR InParanoid; P32722; -.
DR OMA; KWSMIAL; -.
DR PhylomeDB; P32722; -.
DR BioCyc; PAER208964:G1FZ6-979-MON; -.
DR EvolutionaryTrace; P32722; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0045203; C:integral component of cell outer membrane; IDA:UniProtKB.
DR GO; GO:0019867; C:outer membrane; IDA:PseudoCAP.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0015288; F:porin activity; IDA:UniProtKB.
DR GO; GO:0008236; F:serine-type peptidase activity; IDA:UniProtKB.
DR GO; GO:0015802; P:basic amino acid transport; IDA:UniProtKB.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR005318; OM_porin_bac.
DR InterPro; IPR023614; Porin_dom_sf.
DR PANTHER; PTHR34596; PTHR34596; 1.
DR Pfam; PF03573; OprD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Hydrolase;
KW Ion transport; Membrane; Porin; Protease; Reference proteome;
KW Serine protease; Signal; Transmembrane; Transmembrane beta strand;
KW Transport.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:1427017,
FT ECO:0000269|PubMed:8012497"
FT CHAIN 24..443
FT /note="Porin D"
FT /id="PRO_0000027336"
FT ACT_SITE 179
FT /evidence="ECO:0000269|PubMed:9636669"
FT ACT_SITE 231
FT /evidence="ECO:0000269|PubMed:9636669"
FT ACT_SITE 319
FT /evidence="ECO:0000269|PubMed:9636669"
FT MUTAGEN 179
FT /note="H->Q: Loss of protease activity. No effect on porin
FT activity."
FT /evidence="ECO:0000269|PubMed:9636669"
FT MUTAGEN 231
FT /note="D->N: Loss of protease activity. No effect on porin
FT activity."
FT /evidence="ECO:0000269|PubMed:9636669"
FT MUTAGEN 319
FT /note="S->A: Loss of protease activity. No effect on porin
FT activity."
FT /evidence="ECO:0000269|PubMed:9636669"
FT MUTAGEN 390
FT /note="H->Q: No effect on protease activity."
FT /evidence="ECO:0000269|PubMed:9636669"
FT CONFLICT 44
FT /note="L -> Y (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:3SY7"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 41..54
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 62..74
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 79..98
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 119..131
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 134..141
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 160..167
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 173..182
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3SY7"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 202..217
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 220..229
FT /evidence="ECO:0007829|PDB:3SY7"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 233..247
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 250..263
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 273..285
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 288..301
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 337..346
FT /evidence="ECO:0007829|PDB:3SY7"
FT TURN 348..351
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 355..367
FT /evidence="ECO:0007829|PDB:3SY7"
FT HELIX 377..381
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 386..400
FT /evidence="ECO:0007829|PDB:3SY7"
FT TURN 405..408
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 410..420
FT /evidence="ECO:0007829|PDB:3SY7"
FT HELIX 422..424
FT /evidence="ECO:0007829|PDB:3SY7"
FT STRAND 429..439
FT /evidence="ECO:0007829|PDB:3SY7"
SQ SEQUENCE 443 AA; 48360 MW; E083FFE074DCFB64 CRC64;
MKVMKWSAIA LAVSAGSTQF AVADAFVSDQ AEAKGFIEDS SLDLLLRNYY FNRDGKSGSG
DRVDWTQGFL TTYESGFTQG TVGFGVDAFG YLGLKLDGTS DKTGTGNLPV MNDGKPRDDY
SRAGGAVKVR ISKTMLKWGE MQPTAPVFAA GGSRLFPQTA TGFQLQSSEF EGLDLEAGHF
TEGKEPTTVK SRGELYATYA GETAKSADFI GGRYAITDNL SASLYGAELE DIYRQYYLNS
NYTIPLASDQ SLGFDFNIYR TNDEGKAKAG DISNTTWSLA AAYTLDAHTF TLAYQKVHGD
QPFDYIGFGR NGSGAGGDSI FLANSVQYSD FNGPGEKSWQ ARYDLNLASY GVPGLTFMVR
YINGKDIDGT KMSDNNVGYK NYGYGEDGKH HETNLEAKYV VQSGPAKDLS FRIRQAWHRA
NADQGEGDQN EFRLIVDYPL SIL
