PORF_PSEAE
ID PORF_PSEAE Reviewed; 350 AA.
AC P13794;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Outer membrane porin F;
DE Flags: Precursor;
GN Name=oprF; OrderedLocusNames=PA1777;
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], PROTEIN SEQUENCE OF 25-37; 39-53; 79-84;
RP 189-202; 253-259; 261-267; 297-301; 315-318; 325-334 AND 340-345, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=ATCC 33354, and ATCC 33359;
RX PubMed=2447060; DOI=10.1128/jb.170.1.155-162.1988;
RA Duchene M., Schweizer A., Lottspeich F., Krauss G., Marget M., Vogel K.,
RA von Specht B.-U., Domdey H.;
RT "Sequence and transcriptional start site of the Pseudomonas aeruginosa
RT outer membrane porin protein F gene.";
RL J. Bacteriol. 170:155-162(1988).
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 PROTEIN SEQUENCE OF 145-154; 261-291; 302-335 AND 340-350.
RC STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
RN [4] {ECO:0007744|PDB:4RLC}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 25-184, AND DOMAIN.
RX PubMed=25846137; DOI=10.1016/j.jmb.2015.03.016;
RA Zahn M., D'Agostino T., Eren E., Basle A., Ceccarelli M., van den Berg B.;
RT "Small-molecule transport by CarO, an abundant eight-stranded beta-barrel
RT outer membrane protein from Acinetobacter baumannii.";
RL J. Mol. Biol. 427:2329-2339(2015).
RN [5] {ECO:0007744|PDB:5U1H}
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 231-350.
RA Watanabe N.;
RT "Crystal structure of the C-terminal peptidoglycan binding domain of OprF
RT (PA1777) from Pseudomonas aeruginosa.";
RL Submitted (NOV-2016) to the PDB data bank.
CC -!- FUNCTION: Has porin activity, forming small water-filled channels. Also
CC has a structural role in determining cell shape and ability to grow in
CC low-osmolarity medium. {ECO:0000250|UniProtKB:P0A910}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:2447060};
CC Multi-pass membrane protein {ECO:0000305|PubMed:25846137}.
CC -!- DOMAIN: The N-terminal beta-barrel domain (residues 25-184) when
CC reconstituted into lipid vesicles is blocked at both ends.
CC {ECO:0000269|PubMed:25846137}.
CC -!- PTM: Might contain two disulfide bonds. {ECO:0000305|PubMed:2447060}.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
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; AF027290; AAD11568.1; -; Genomic_DNA.
DR EMBL; M18975; AAA25973.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG05166.1; -; Genomic_DNA.
DR PIR; S39156; S39156.
DR RefSeq; NP_250468.1; NC_002516.2.
DR RefSeq; WP_003087843.1; NZ_QZGE01000003.1.
DR PDB; 4RLC; X-ray; 1.60 A; A=25-184.
DR PDB; 5U1H; X-ray; 1.50 A; A/B/C/D=231-350.
DR PDBsum; 4RLC; -.
DR PDBsum; 5U1H; -.
DR AlphaFoldDB; P13794; -.
DR SMR; P13794; -.
DR STRING; 287.DR97_109; -.
DR ChEMBL; CHEMBL4523189; -.
DR TCDB; 1.B.6.1.2; the ompa-ompf porin (oop) family.
DR PaxDb; P13794; -.
DR PRIDE; P13794; -.
DR DNASU; 878442; -.
DR EnsemblBacteria; AAG05166; AAG05166; PA1777.
DR GeneID; 878442; -.
DR KEGG; pae:PA1777; -.
DR PATRIC; fig|208964.12.peg.1842; -.
DR PseudoCAP; PA1777; -.
DR HOGENOM; CLU_031536_2_0_6; -.
DR InParanoid; P13794; -.
DR OMA; ADFMQQY; -.
DR PhylomeDB; P13794; -.
DR BioCyc; PAER208964:G1FZ6-1808-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019867; C:outer membrane; TAS:PseudoCAP.
DR GO; GO:0046930; C:pore complex; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0001851; F:complement component C3b binding; IPI:PseudoCAP.
DR GO; GO:0015288; F:porin activity; TAS:PseudoCAP.
DR GO; GO:0044406; P:adhesion of symbiont to host; IMP:PseudoCAP.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR CDD; cd07185; OmpA_C-like; 1.
DR Gene3D; 3.30.1330.60; -; 1.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR006664; OMP_bac.
DR InterPro; IPR006665; OmpA-like.
DR InterPro; IPR006690; OMPA-like_CS.
DR InterPro; IPR036737; OmpA-like_sf.
DR InterPro; IPR008722; OprF_membrane_N.
DR InterPro; IPR028974; TSP_type-3_rpt.
DR Pfam; PF00691; OmpA; 1.
DR Pfam; PF05736; OprF; 1.
DR PRINTS; PR01021; OMPADOMAIN.
DR SUPFAM; SSF103088; SSF103088; 1.
DR SUPFAM; SSF103647; SSF103647; 1.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS01068; OMPA_1; 1.
DR PROSITE; PS51123; OMPA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Cell shape; Direct protein sequencing;
KW Disulfide bond; Ion transport; Membrane; Porin; Reference proteome; Repeat;
KW Signal; Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:2447060"
FT CHAIN 25..350
FT /note="Outer membrane porin F"
FT /id="PRO_0000020115"
FT REPEAT 190..191
FT /note="1"
FT REPEAT 192..193
FT /note="2"
FT REPEAT 194..195
FT /note="3"
FT DOMAIN 231..349
FT /note="OmpA-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00473"
FT REGION 190..195
FT /note="3 X 2 AA tandem repeats of X-P"
FT STRAND 30..39
FT /evidence="ECO:0007829|PDB:4RLC"
FT STRAND 51..75
FT /evidence="ECO:0007829|PDB:4RLC"
FT STRAND 89..100
FT /evidence="ECO:0007829|PDB:4RLC"
FT STRAND 104..124
FT /evidence="ECO:0007829|PDB:4RLC"
FT STRAND 129..162
FT /evidence="ECO:0007829|PDB:4RLC"
FT STRAND 173..184
FT /evidence="ECO:0007829|PDB:4RLC"
FT STRAND 231..243
FT /evidence="ECO:0007829|PDB:5U1H"
FT HELIX 253..255
FT /evidence="ECO:0007829|PDB:5U1H"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:5U1H"
FT STRAND 274..278
FT /evidence="ECO:0007829|PDB:5U1H"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:5U1H"
FT HELIX 286..306
FT /evidence="ECO:0007829|PDB:5U1H"
FT HELIX 312..314
FT /evidence="ECO:0007829|PDB:5U1H"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:5U1H"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:5U1H"
FT STRAND 339..348
FT /evidence="ECO:0007829|PDB:5U1H"
SQ SEQUENCE 350 AA; 37640 MW; D1F758F076874383 CRC64;
MKLKNTLGVV IGSLVAASAM NAFAQGQNSV EIEAFGKRYF TDSVRNMKNA DLYGGSIGYF
LTDDVELALS YGEYHDVRGT YETGNKKVHG NLTSLDAIYH FGTPGVGLRP YVSAGLAHQN
ITNINSDSQG RQQMTMANIG AGLKYYFTEN FFAKASLDGQ YGLEKRDNGH QGEWMAGLGV
GFNFGGSKAA PAPEPVADVC SDSDNDGVCD NVDKCPDTPA NVTVDANGCP AVAEVVRVQL
DVKFDFDKSK VKENSYADIK NLADFMKQYP STSTTVEGHT DSVGTDAYNQ KLSERRANAV
RDVLVNEYGV EGGRVNAVGY GESRPVADNA TAEGRAINRR VEAEVEAEAK
