OMPC_SALTI
ID OMPC_SALTI Reviewed; 378 AA.
AC P0A264; O52503; P09878;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Outer membrane porin C;
DE AltName: Full=Outer membrane protein C;
DE AltName: Full=Porin OmpC;
DE Flags: Precursor;
GN Name=ompC; OrderedLocusNames=STY2493, t0597;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2684785; DOI=10.1016/0378-1119(89)90105-4;
RA Puente J.L., Alvarez-Scherer V., Gosset G., Calva E.;
RT "Comparative analysis of the Salmonella typhi and Escherichia coli ompC
RT genes.";
RL Gene 83:197-206(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=3412902; DOI=10.1093/nar/16.15.7721;
RA Venegas A., Gomez I., Zaror I., Yudelevich A.;
RT "The nucleotide sequence of the Salmonella typhi ompC porin gene.";
RL Nucleic Acids Res. 16:7721-7721(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
RN [5]
RP SUBCELLULAR LOCATION, AND INDUCTION.
RC STRAIN=ATCC 700931 / Ty2 / CVD908;
RX PubMed=8063417; DOI=10.1128/iai.62.9.3984-3993.1994;
RA Pickard D.J., Li J., Roberts M.R., Maskell D., Hone D., Levine M.,
RA Dougan G., Chatfield S.;
RT "Characterization of defined ompR mutants of Salmonella typhi: ompR is
RT involved in the regulation of Vi polysaccharide expression.";
RL Infect. Immun. 62:3984-3993(1994).
RN [6]
RP 3D-STRUCTURE MODELING, AND CRYSTALLIZATION.
RX PubMed=10405180; DOI=10.1016/s0014-5793(99)00746-2;
RA Arockiasamy A., Krishnaswamy S.;
RT "Crystallization of the immunodominant outer membrane protein OmpC; the
RT first protein crystals from Salmonella typhi, a human pathogen.";
RL FEBS Lett. 453:380-382(1999).
RN [7] {ECO:0007744|PDB:3UPG}
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 22-378.
RC STRAIN=Ty21a;
RA Prasanth P., Putcha B.K., Arockiasamy A., Krishnaswamy S.;
RT "Crystal structure of osmoporin (OmpC) loop deletion mutant: an outer
RT membrane protein from Salmonella typhi.";
RL Submitted (NOV-2011) to the PDB data bank.
RN [8] {ECO:0007744|PDB:3UU2}
RP X-RAY CRYSTALLOGRAPHY (3.59 ANGSTROMS) OF 22-378, AND SUBUNIT.
RC STRAIN=Ty21a;
RA Prasanth P., Putcha B.K., Arockiasamy A., Krishnaswamy S.;
RT "Crystal Structure of outer membrane protein OmpC from Salmonella typhi.";
RL Submitted (NOV-2011) to the PDB data bank.
CC -!- FUNCTION: Forms pores that allow passive diffusion of small molecules
CC across the outer membrane. {ECO:0000305}.
CC -!- SUBUNIT: Homotrimer (Ref.8). Forms mixed heterotrimers with OmpF and
CC with PhoE; other mixed heterotrimers with other porins are also
CC probable (By similarity). {ECO:0000250|UniProtKB:P06996,
CC ECO:0000269|Ref.8}.
CC -!- SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000269|PubMed:8063417};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P06996}.
CC -!- INDUCTION: Unlike E.coli or S.typhimurium both OmpC and OmpF porins are
CC expressed constitutively, i.e. at both high and low osmolarity, under
CC control of OmpR (at protein level). {ECO:0000269|PubMed:8063417}.
CC -!- SIMILARITY: Belongs to the Gram-negative porin family. {ECO:0000305}.
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DR EMBL; X07835; CAA30688.1; -; Genomic_DNA.
DR EMBL; AL513382; CAD07499.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68302.1; -; Genomic_DNA.
DR PIR; JQ0119; MMEBPC.
DR RefSeq; NP_456812.1; NC_003198.1.
DR RefSeq; WP_000865526.1; NZ_WSUR01000051.1.
DR PDB; 3UPG; X-ray; 3.20 A; A=22-378.
DR PDB; 3UU2; X-ray; 3.59 A; A/B/C=22-378.
DR PDBsum; 3UPG; -.
DR PDBsum; 3UU2; -.
DR AlphaFoldDB; P0A264; -.
DR SMR; P0A264; -.
DR STRING; 220341.16503494; -.
DR EnsemblBacteria; AAO68302; AAO68302; t0597.
DR KEGG; stt:t0597; -.
DR KEGG; sty:STY2493; -.
DR PATRIC; fig|220341.7.peg.2525; -.
DR eggNOG; COG3203; Bacteria.
DR HOGENOM; CLU_058202_0_0_6; -.
DR OMA; DNKENSW; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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: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; Ion transport; Membrane; Porin; Signal;
KW Transmembrane; Transmembrane beta strand; Transport.
FT SIGNAL 1..21
FT CHAIN 22..378
FT /note="Outer membrane porin C"
FT /id="PRO_0000025234"
FT CONFLICT 362
FT /note="Missing (in Ref. 2; CAA30688)"
FT /evidence="ECO:0000305"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 30..33
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:3UPG"
FT TURN 48..50
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 68..85
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 92..103
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:3UPG"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:3UPG"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:3UPG"
FT TURN 156..160
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 164..171
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 204..215
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 238..248
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 251..261
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:3UPG"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 299..309
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 325..339
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 342..351
FT /evidence="ECO:0007829|PDB:3UPG"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:3UPG"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:3UPG"
SQ SEQUENCE 378 AA; 41239 MW; 58479E8685B43ED1 CRC64;
MKVKVLSLLV PALLVAGAAN AAEIYNKDGN KLDLFGKVDG LHYFSDDKGS DGDQTYMRIG
FKGETQVNDQ LTGYGQWEYQ IQGNQTEGSN DSWTRVAFAG LKFADAGSFD YGRNYGVTYD
VTSWTDVLPE FGGDTYGADN FMQQRGNGYA TYRNTDFFGL VDGLDFALQY QGKNGSVSGE
NTNGRSLLNQ NGDGYGGSLT YAIGEGFSVG GAITTSKRTA DQNNTANARL YGNGDRATVY
TGGLKYDANN IYLAAQYSQT YNATRFGTSN GSNPSTSYGF ANKAQNFEVV AQYQFDFGLR
PSVAYLQSKG KDISNGYGAS YGDQDIVKYV DVGATYYFNK NMSTYVDYKI NLLDKNDFTR
DAGINTDDIV ALGLVYQF
