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PORI_FUSBL
ID   PORI_FUSBL              Reviewed;         289 AA.
AC   P39767;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Porin;
GN   Name=opmA;
OS   Fuscovulum blasticum (Rhodobacter blasticus) (Rhodopseudomonas blastica).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Fuscovulum.
OX   NCBI_TaxID=1075;
RN   [1]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=8142898; DOI=10.1002/pro.5560030108;
RA   Kreusch A., Neubueser A., Schiltz E., Weckesser J., Schulz G.E.;
RT   "Structure of the membrane channel porin from Rhodopseudomonas blastica at
RT   2.0-A resolution.";
RL   Protein Sci. 3:58-63(1994).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS).
RX   PubMed=7525973; DOI=10.1006/jmbi.1994.1690;
RA   Kreusch A., Schulz G.E.;
RT   "Refined structure of the porin from Rhodopseudomonas blastica. Comparison
RT   with the porin from Rhodobacter capsulatus.";
RL   J. Mol. Biol. 243:891-905(1994).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS.
RX   PubMed=9684893; DOI=10.1002/pro.5560070714;
RA   Schmid B., Maveyraud L., Kromer M., Schulz G.E.;
RT   "Porin mutants with new channel properties.";
RL   Protein Sci. 7:1603-1611(1998).
CC   -!- FUNCTION: Forms channels that allow the passive diffusion of small
CC       hydrophilic solutes up to an exclusion limit of about 0.6 kDa.
CC   -!- SUBUNIT: Homotrimer.
CC   -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
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DR   PIR; S38806; S38806.
DR   PDB; 1BH3; X-ray; 2.19 A; A=2-289.
DR   PDB; 1H6S; X-ray; 3.00 A; 1=1-289.
DR   PDB; 1PRN; X-ray; 1.96 A; A=1-289.
DR   PDB; 2PRN; X-ray; 1.93 A; A=2-289.
DR   PDB; 3PRN; X-ray; 1.90 A; A=2-289.
DR   PDB; 5PRN; X-ray; 2.00 A; A=2-289.
DR   PDB; 6PRN; X-ray; 2.04 A; A=2-289.
DR   PDB; 7PRN; X-ray; 2.25 A; A=2-289.
DR   PDB; 8PRN; X-ray; 2.30 A; A=2-289.
DR   PDBsum; 1BH3; -.
DR   PDBsum; 1H6S; -.
DR   PDBsum; 1PRN; -.
DR   PDBsum; 2PRN; -.
DR   PDBsum; 3PRN; -.
DR   PDBsum; 5PRN; -.
DR   PDBsum; 6PRN; -.
DR   PDBsum; 7PRN; -.
DR   PDBsum; 8PRN; -.
DR   AlphaFoldDB; P39767; -.
DR   SMR; P39767; -.
DR   DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR   TCDB; 1.B.7.1.3; the rhodobacter porca porin (rpp) family.
DR   EvolutionaryTrace; P39767; -.
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; IPR033900; Gram_neg_porin_domain.
DR   InterPro; IPR023614; Porin_dom_sf.
DR   Pfam; PF13609; Porin_4; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell outer membrane; Ion transport; Membrane; Porin;
KW   Transmembrane; Transmembrane beta strand; Transport.
FT   CHAIN           1..289
FT                   /note="Porin"
FT                   /id="PRO_0000198029"
FT   STRAND          2..15
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          24..39
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          46..56
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   HELIX           60..62
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          70..75
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          78..84
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   HELIX           88..91
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   TURN            95..98
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   TURN            101..104
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   TURN            126..129
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          131..138
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          140..150
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   TURN            151..154
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   HELIX           157..159
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          163..171
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          173..184
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   HELIX           185..187
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          193..200
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          203..214
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          222..232
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          235..244
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          252..262
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          265..273
FT                   /evidence="ECO:0007829|PDB:3PRN"
FT   STRAND          279..288
FT                   /evidence="ECO:0007829|PDB:3PRN"
SQ   SEQUENCE   289 AA;  30597 MW;  08252D9803A1044C CRC64;
     EISLNGYGRF GLQYVEDRGV GLEDTIISSR LRINIVGTTE TDQGVTFGAK LRMQWDDGDA
     FAGTAGNAAQ FWTSYNGVTV SVGNVDTAFD SVALTYDSEM GYEASSFGDA QSSFFAYNSK
     YDASGALDNY NGIAVTYSIS GVNLYLSYVD PDQTVDSSLV TEEFGIAADW SNDMISLAAA
     YTTDAGGIVD NDIAFVGAAY KFNDAGTVGL NWYDNGLSTA GDQVTLYGNY AFGATTVRAY
     VSDIDRAGAD TAYGIGADYQ FAEGVKVSGS VQSGFANETV ADVGVRFDF
 
 
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