OMPC_KLEPN
ID OMPC_KLEPN Reviewed; 363 AA.
AC Q48473;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 102.
DE RecName: Full=Outer membrane porin C;
DE AltName: Full=Outer membrane protein C;
DE AltName: Full=Porin OmpC;
DE AltName: Full=Porin ompk36;
DE Flags: Precursor;
GN Name=ompC; Synonyms=ompK36;
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=C3;
RX PubMed=7868262; DOI=10.1128/iai.63.3.903-910.1995;
RA Alberti S., Rodriquez-Quinones F., Schirmer T., Rummel G., Tomas J.M.,
RA Rosenbusch J.P., Benedi V.J.;
RT "A porin from Klebsiella pneumoniae: sequence homology, three-dimensional
RT model, and complement binding.";
RL Infect. Immun. 63:903-910(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS).
RX PubMed=10196126; DOI=10.1016/s0969-2126(99)80055-0;
RA Dutzler R., Rummel G., Alberti S., Hernandez-Alles S., Phale P.S.,
RA Rosenbusch J.P., Benedi V.J., Schirmer T.;
RT "Crystal structure and functional characterization of OmpK36, the osmoporin
RT of Klebsiella pneumoniae.";
RL Structure 7:425-434(1999).
CC -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC across the outer membrane. In K.pneumoniae it has been shown to bind
CC the C1Q component and activate the classical pathway of the complement
CC system.
CC -!- SUBUNIT: Homotrimer.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; Z33506; CAA83913.1; -; Genomic_DNA.
DR PIR; S51104; S51104.
DR PDB; 1OSM; X-ray; 3.20 A; A/B/C=22-363.
DR PDBsum; 1OSM; -.
DR AlphaFoldDB; Q48473; -.
DR SMR; Q48473; -.
DR PRIDE; Q48473; -.
DR EvolutionaryTrace; Q48473; -.
DR PHI-base; PHI:2872; -.
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:0034220; P:ion transmembrane transport; IEA:InterPro.
DR Gene3D; 2.40.160.10; -; 1.
DR InterPro; IPR023614; Porin_dom_sf.
DR InterPro; IPR001897; Porin_gammaproteobac.
DR InterPro; IPR001702; Porin_Gram-ve.
DR InterPro; IPR013793; Porin_Gram-ve_CS.
DR Pfam; PF00267; Porin_1; 1.
DR PRINTS; PR00183; ECOLIPORIN.
DR PRINTS; PR00182; ECOLNEIPORIN.
DR PROSITE; PS00576; GRAM_NEG_PORIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing;
KW Ion transport; Membrane; Porin; Signal; Transmembrane;
KW Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT CHAIN 22..363
FT /note="Outer membrane porin C"
FT /id="PRO_0000025236"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 30..47
FT /evidence="ECO:0007829|PDB:1OSM"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 72..82
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 93..103
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 109..116
FT /evidence="ECO:0007829|PDB:1OSM"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:1OSM"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 144..157
FT /evidence="ECO:0007829|PDB:1OSM"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:1OSM"
FT TURN 180..182
FT /evidence="ECO:0007829|PDB:1OSM"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 196..207
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 210..220
FT /evidence="ECO:0007829|PDB:1OSM"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 234..247
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 250..261
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 263..265
FT /evidence="ECO:0007829|PDB:1OSM"
FT TURN 266..268
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 272..283
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 288..301
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 308..324
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 327..336
FT /evidence="ECO:0007829|PDB:1OSM"
FT HELIX 342..347
FT /evidence="ECO:0007829|PDB:1OSM"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:1OSM"
SQ SEQUENCE 363 AA; 39663 MW; 9DE45546F01F116C CRC64;
MKVKVLSLLV PALLVAGAAN AAEIYNKDGN KLDLYGKIDG LHYFSDDKDV DGDQTYMRLG
VKGETQINDQ LTGYGQWEYN VQANNTESSS DQAWTRLAFA GLKFGDAGSF DYGRNYGVVY
DVTSWTDVLP EFGGDTYGSD NFLQSRANGV ATYRNSDFFG LVDGLNFALQ YQGKNGSVSG
EGATNNGRGA LKQNGDGFGT SVTYDIFDGI SAGFAYANSK RTDDQNQLLL GEGDHAETYT
GGLKYDANNI YLATQYTQTY NATRAGSLGF ANKAQNFEVA AQYQFDFGLR PSVAYLQSKG
KDLNGYGDQD ILKYVDVGAT YYFNKNMSTY VDYKINLLDD NSFTRSAGIS TDDVVALGLV
YQF
