OMPX_ECOLI
ID OMPX_ECOLI Reviewed; 171 AA.
AC P0A917; P36546;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Outer membrane protein X;
DE Flags: Precursor;
GN Name=ompX; Synonyms=ybiG; OrderedLocusNames=b0814, JW0799;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7836315; DOI=10.1128/jb.177.3.799-804.1995;
RA Mecsas J., Welch R., Erickson J.W., Gross C.A.;
RT "Identification and characterization of an outer membrane protein, OmpX, in
RT Escherichia coli that is homologous to a family of outer membrane proteins
RT including Ail of Yersinia enterocolitica.";
RL J. Bacteriol. 177:799-804(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-137.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8021175; DOI=10.1128/jb.176.13.3928-3935.1994;
RA Lomovskaya O.L., Kidwell J.P., Matin A.;
RT "Characterization of the sigma 38-dependent expression of a core
RT Escherichia coli starvation gene, pexB.";
RL J. Bacteriol. 176:3928-3935(1994).
RN [6]
RP PROTEIN SEQUENCE OF 24-28.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9629924; DOI=10.1002/elps.1150190539;
RA Molloy M.P., Herbert B.R., Walsh B.J., Tyler M.I., Traini M.,
RA Sanchez J.-C., Hochstrasser D.F., Williams K.L., Gooley A.A.;
RT "Extraction of membrane proteins by differential solubilization for
RT separation using two-dimensional gel electrophoresis.";
RL Electrophoresis 19:837-844(1998).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 24-171.
RX PubMed=10545325; DOI=10.1016/s0969-2126(00)80063-5;
RA Vogt J., Schulz G.E.;
RT "The structure of the outer membrane protein OmpX from Escherichia coli
RT reveals possible mechanisms of virulence.";
RL Structure 7:1301-1309(1999).
CC -!- INTERACTION:
CC P0A917; P0AEU7: skp; NbExp=2; IntAct=EBI-552413, EBI-548242;
CC -!- SUBCELLULAR LOCATION: Cell outer membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the outer membrane OOP (TC 1.B.6) superfamily.
CC OmpX family. {ECO:0000305}.
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DR EMBL; L37088; AAA66329.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73901.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35486.1; -; Genomic_DNA.
DR EMBL; U04242; AAA21856.1; -; Genomic_DNA.
DR PIR; I55173; I55173.
DR RefSeq; NP_415335.1; NC_000913.3.
DR RefSeq; WP_001295296.1; NZ_STEB01000019.1.
DR PDB; 1ORM; NMR; -; A=24-171.
DR PDB; 1Q9F; NMR; -; A=24-171.
DR PDB; 1Q9G; NMR; -; A=24-171.
DR PDB; 1QJ8; X-ray; 1.90 A; A=24-171.
DR PDB; 1QJ9; X-ray; 2.10 A; A=24-171.
DR PDB; 2M06; NMR; -; A=24-171.
DR PDB; 2M07; NMR; -; A=24-171.
DR PDB; 2MNH; NMR; -; A=24-171.
DR PDBsum; 1ORM; -.
DR PDBsum; 1Q9F; -.
DR PDBsum; 1Q9G; -.
DR PDBsum; 1QJ8; -.
DR PDBsum; 1QJ9; -.
DR PDBsum; 2M06; -.
DR PDBsum; 2M07; -.
DR PDBsum; 2MNH; -.
DR AlphaFoldDB; P0A917; -.
DR BMRB; P0A917; -.
DR SMR; P0A917; -.
DR BioGRID; 4261010; 284.
DR DIP; DIP-48016N; -.
DR IntAct; P0A917; 3.
DR MINT; P0A917; -.
DR STRING; 511145.b0814; -.
DR DrugBank; DB04233; (Hydroxyethyloxy)Tri(Ethyloxy)Octane.
DR TCDB; 1.B.6.2.1; the ompa-ompf porin (oop) family.
DR SWISS-2DPAGE; P0A917; -.
DR jPOST; P0A917; -.
DR PaxDb; P0A917; -.
DR PRIDE; P0A917; -.
DR EnsemblBacteria; AAC73901; AAC73901; b0814.
DR EnsemblBacteria; BAA35486; BAA35486; BAA35486.
DR GeneID; 66670913; -.
DR GeneID; 944967; -.
DR KEGG; ecj:JW0799; -.
DR KEGG; eco:b0814; -.
DR PATRIC; fig|1411691.4.peg.1464; -.
DR EchoBASE; EB2056; -.
DR eggNOG; COG3637; Bacteria.
DR HOGENOM; CLU_099385_1_0_6; -.
DR OMA; RFNDWAS; -.
DR PhylomeDB; P0A917; -.
DR BioCyc; EcoCyc:EG12117-MON; -.
DR EvolutionaryTrace; P0A917; -.
DR PHI-base; PHI:6250; -.
DR PRO; PR:P0A917; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0009279; C:cell outer membrane; IDA:EcoCyc.
DR GO; GO:0044384; C:host outer membrane; IEA:InterPro.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR InterPro; IPR000758; Enterovir_OMP.
DR InterPro; IPR011250; OMP/PagP_b-brl.
DR InterPro; IPR027385; OMP_b-brl.
DR Pfam; PF13505; OMP_b-brl; 1.
DR PRINTS; PR00316; ENTEROVIROMP.
DR SUPFAM; SSF56925; SSF56925; 1.
DR PROSITE; PS00694; ENT_VIR_OMP_1; 1.
DR PROSITE; PS00695; ENT_VIR_OMP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell outer membrane; Direct protein sequencing; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane beta strand.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:9629924"
FT CHAIN 24..171
FT /note="Outer membrane protein X"
FT /id="PRO_0000020199"
FT TOPO_DOM 24..25
FT /note="Periplasmic"
FT TRANSMEM 26..35
FT /note="Beta stranded"
FT TOPO_DOM 36..44
FT /note="Extracellular"
FT TRANSMEM 45..54
FT /note="Beta stranded"
FT TOPO_DOM 55..59
FT /note="Periplasmic"
FT TRANSMEM 60..69
FT /note="Beta stranded"
FT TOPO_DOM 70..85
FT /note="Extracellular"
FT TRANSMEM 86..95
FT /note="Beta stranded"
FT TOPO_DOM 96..99
FT /note="Periplasmic"
FT TRANSMEM 100..109
FT /note="Beta stranded"
FT TOPO_DOM 110..129
FT /note="Extracellular"
FT TRANSMEM 130..139
FT /note="Beta stranded"
FT TOPO_DOM 140..143
FT /note="Periplasmic"
FT TRANSMEM 144..153
FT /note="Beta stranded"
FT TOPO_DOM 154..160
FT /note="Extracellular"
FT TRANSMEM 161..170
FT /note="Beta stranded"
FT TOPO_DOM 171
FT /note="Periplasmic"
FT CONFLICT 10
FT /note="L -> M (in Ref. 5; AAA21856)"
FT /evidence="ECO:0000305"
FT STRAND 25..37
FT /evidence="ECO:0007829|PDB:1QJ8"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1QJ8"
FT STRAND 41..54
FT /evidence="ECO:0007829|PDB:1QJ8"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:1ORM"
FT STRAND 59..74
FT /evidence="ECO:0007829|PDB:1QJ8"
FT STRAND 75..77
FT /evidence="ECO:0007829|PDB:1ORM"
FT STRAND 80..97
FT /evidence="ECO:0007829|PDB:1QJ8"
FT STRAND 100..117
FT /evidence="ECO:0007829|PDB:1QJ8"
FT TURN 118..120
FT /evidence="ECO:0007829|PDB:1QJ8"
FT STRAND 121..138
FT /evidence="ECO:0007829|PDB:1QJ8"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:1ORM"
FT STRAND 144..155
FT /evidence="ECO:0007829|PDB:1QJ8"
FT STRAND 158..170
FT /evidence="ECO:0007829|PDB:1QJ8"
SQ SEQUENCE 171 AA; 18603 MW; 77CE1245DAE81462 CRC64;
MKKIACLSAL AAVLAFTAGT SVAATSTVTG GYAQSDAQGQ MNKMGGFNLK YRYEEDNSPL
GVIGSFTYTE KSRTASSGDY NKNQYYGITA GPAYRINDWA SIYGVVGVGY GKFQTTEYPT
YKHDTSDYGF SYGAGLQFNP MENVALDFSY EQSRIRSVDV GTWIAGVGYR F
