RegulonDB

RegulonDB RegulonDB 11.1: Gene Form

ompG gene in Escherichia coli K-12 genome

Gene local context to scale (view description)

Gene
Name:	ompG
Synonym(s):	ECK1315, G6657, b1319
Genome position(nucleotides):	1381947 --> 1382852
Strand:	forward
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	49.89
External database links:

ASAP:	ABE-0004425
ECHOBASE:	EB3202
ECOLIHUB:	ompG
OU-MICROARRAY:	b1319
STRING:	511145.b1319
COLOMBOS:	ompG

Product

Name:

outer membrane porin G

Synonym(s):

OmpG

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

outer membrane

Molecular weight:

34.913

Isoelectric point:

4.215

Motif(s):

Type	Positions	Sequence	Comment
	1 -> 21	MKKLLPCTALVMCAGMACAQA
	22 -> 301	EERNDWHFNIGAMYEIENVEGYGEDMDGLAEPSVYFNAANGPWRIALAYYQEGPVDYSAGKRGTWFDRPELEVHYQFLENDDFSFGLTGGFRNYGYHYVDEPGKDTANMQRWKIAPDWDVKLTDDLRFNGWLSMYKFANDLNTTGYADTRVETETGLQYTFNETVALRVNYYLERGFNMDDSRNNGEFSTQEIRAYLPLTLGNHSVTPYTRIGLDRWSNWDWQDDIEREGHDFNRVGLFYGYDFQNGLSVSLEYAFEWQDHDEGDSDKFHYAGVGVNYSF	UniProt: Outer membrane porin G.
	25 -> 299	NDWHFNIGAMYEIENVEGYGEDMDGLAEPSVYFNAANGPWRIALAYYQEGPVDYSAGKRGTWFDRPELEVHYQFLENDDFSFGLTGGFRNYGYHYVDEPGKDTANMQRWKIAPDWDVKLTDDLRFNGWLSMYKFANDLNTTGYADTRVETETGLQYTFNETVALRVNYYLERGFNMDDSRNNGEFSTQEIRAYLPLTLGNHSVTPYTRIGLDRWSNWDWQDDIEREGHDFNRVGLFYGYDFQNGLSVSLEYAFEWQDHDEGDSDKFHYAGVGVNY
	27 -> 35	WHFNIGAMY	UniProt: Beta stranded.
	28 -> 36	HFNIGAMYE	predicted transmembrane β strand

Type	Positions	Sequence	Comment
	1 -> 21	MKKLLPCTALVMCAGMACAQA
	22 -> 301	EERNDWHFNIGAMYEIENVEGYGEDMDGLAEPSVYFNAANGPWRIALAYYQEGPVDYSAGKRGTWFDRPELEVHYQFLENDDFSFGLTGGFRNYGYHYVDEPGKDTANMQRWKIAPDWDVKLTDDLRFNGWLSMYKFANDLNTTGYADTRVETETGLQYTFNETVALRVNYYLERGFNMDDSRNNGEFSTQEIRAYLPLTLGNHSVTPYTRIGLDRWSNWDWQDDIEREGHDFNRVGLFYGYDFQNGLSVSLEYAFEWQDHDEGDSDKFHYAGVGVNYSF	UniProt: Outer membrane porin G.
	25 -> 299	NDWHFNIGAMYEIENVEGYGEDMDGLAEPSVYFNAANGPWRIALAYYQEGPVDYSAGKRGTWFDRPELEVHYQFLENDDFSFGLTGGFRNYGYHYVDEPGKDTANMQRWKIAPDWDVKLTDDLRFNGWLSMYKFANDLNTTGYADTRVETETGLQYTFNETVALRVNYYLERGFNMDDSRNNGEFSTQEIRAYLPLTLGNHSVTPYTRIGLDRWSNWDWQDDIEREGHDFNRVGLFYGYDFQNGLSVSLEYAFEWQDHDEGDSDKFHYAGVGVNY
	27 -> 35	WHFNIGAMY	UniProt: Beta stranded.
	28 -> 36	HFNIGAMYE	predicted transmembrane β strand
	37 -> 53	IENVEGYGEDMDGLAEP	predicted extracellular loop
	47 -> 57	MDGLAEPSVYF	UniProt: Beta stranded.
	54 -> 61	SVYFNAAN	predicted transmembrane β strand
	64 -> 71	WRIALAYY	predicted transmembrane β strand
	72 -> 89	QEGPVDYSAGKRGTWFDR	predicted extracellular loop
	89 -> 98	RPELEVHYQF	UniProt: Beta stranded.
	90 -> 99	PELEVHYQFL	predicted transmembrane β strand
	104 -> 112	FSFGLTGGF	UniProt: Beta stranded.
	105 -> 115	SFGLTGGFRNY	predicted transmembrane β strand
	116 -> 129	GYHYVDEPGKDTAN	predicted extracellular loop
	129 -> 136	NMQRWKIA	UniProt: Beta stranded.
	130 -> 142	MQRWKIAPDWDVK	predicted transmembrane β strand
	147 -> 159	LRFNGWLSMYKFA	predicted transmembrane β strand
	149 -> 158	FNGWLSMYKF	UniProt: Beta stranded.
	160 -> 170	NDLNTTGYADT
	171 -> 181	RVETETGLQYT	predicted transmembrane β strand
	172 -> 182	VETETGLQYTF	UniProt: Beta stranded.
	186 -> 195	VALRVNYYLE	UniProt: Beta stranded.
	187 -> 196	ALRVNYYLER	predicted transmembrane β strand
	197 -> 210	GFNMDDSRNNGEFS	predicted extracellular loop
	201 -> 209	DDSRNNGEF	UniProt: Beta stranded.
	211 -> 222	TQEIRAYLPLTL	predicted transmembrane β strand
	213 -> 222	EIRAYLPLTL	UniProt: Beta stranded.
	225 -> 231	HSVTPYT	predicted transmembrane β strand
	230 -> 238	YTRIGLDRW	UniProt: Beta stranded.
	232 -> 257	RIGLDRWSNWDWQDDIEREGHDFNRV	predicted extracellular loop
	240 -> 248	NWDWQDDIE	UniProt: Beta stranded.
	252 -> 252	H	Histidine residue proposed by \|CITS: [16888630]\| to be involved in pH dependent gating ; alternate sequence generated H → A and H → C:
	254 -> 265	FNRVGLFYGYDF	UniProt: Beta stranded.
	258 -> 264	GLFYGYD	predicted transmembrane β strand
	269 -> 279	LSVSLEYAFEW	UniProt: Beta stranded.
	276 -> 293	AFEWQDHDEGDSDKFHYA	predicted extracellular loop
	282 -> 282	H	Histidine residue proposed by \|CITS: [16888630]\| to be involved in pH dependent gating ; alternate sequence generated H → A and H → C:
	289 -> 300	KFHYAGVGVNYS	UniProt: Beta stranded.
	294 -> 300	GVGVNYS	predicted transmembrane β strand

Classification:

Multifun Terms (GenProtEC)
Multifun Terms (GenProtEC)		4 - transport --> 4.1 - Channel-type Transporters --> 4.1.B - Beta barrel porins (The Outer Membrane Porin (OMP) Functional Superfamily)
Gene Ontology Terms (GO)
	cellular_component	GO:0009279 - cell outer membrane GO:0016020 - membrane GO:0016021 - integral component of membrane GO:0045203 - integral component of cell outer membrane GO:0046930 - pore complex
	molecular_function	GO:0015288 - porin activity GO:0015478 - oligosaccharide transporting porin activity GO:0015481 - maltose transporting porin activity
	biological_process	GO:0006811 - ion transport GO:0015768 - maltose transport GO:0015772 - oligosaccharide transport GO:0034219 - carbohydrate transmembrane transport

Note(s):

Note(s): ...[more].

Reference(s):

[1] Anbazhagan V., et al., 2008
[2] Behlau M., et al., 2001
[3] Conlan S., et al., 2003
[4] Conlan S., et al., 2000
[5] Fajardo DA., et al., 1998
[6] Hiller M., et al., 2005
[7] Korkmaz F., et al., 2008
[8] Koster S., et al., 2015
[9] Misra R., et al., 1989
[10] Thoma J., et al., 2018

External database links:

ALPHAFOLD:

DIP:

ECOCYC:

ECOLIWIKI:

INTERPRO:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PDB:

PFAM:

PRIDE:

PRODB:

REFSEQ:

SMR:

UNIPROT:

Operon

Name:

ycjMNOPQRSTUV-ymjB-ompG

Operon arrangement:

Transcription unit	Promoter
ompG
ycjMNOPQRSTUV-ymjB-ompG

RNA cis-regulatory element

Attenuation:	Translational

Elements in the selected gene context region unrelated to any object in RegulonDB

	Type	Name	Post Left	Post Right	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References

Reference(s)
[1] Anbazhagan V., Qu J., Kleinschmidt JH., Marsh D., 2008, Incorporation of outer membrane protein OmpG in lipid membranes: protein-lipid interactions and beta-barrel orientation., Biochemistry 47(23):6189-98
[2] Behlau M., Mills DJ., Quader H., Kuhlbrandt W., Vonck J., 2001, Projection structure of the monomeric porin OmpG at 6 A resolution., J Mol Biol 305(1):71-7
[3] Conlan S., Bayley H., 2003, Folding of a monomeric porin, OmpG, in detergent solution., Biochemistry 42(31):9453-65
[4] Conlan S., Zhang Y., Cheley S., Bayley H., 2000, Biochemical and biophysical characterization of OmpG: A monomeric porin., Biochemistry 39(39):11845-54
[5] Fajardo DA., Cheung J., Ito C., Sugawara E., Nikaido H., Misra R., 1998, Biochemistry and regulation of a novel Escherichia coli K-12 porin protein, OmpG, which produces unusually large channels., J Bacteriol 180(17):4452-9
[6] Hiller M., Krabben L., Vinothkumar KR., Castellani F., van Rossum BJ., Kuhlbrandt W., Oschkinat H., 2005, Solid-state magic-angle spinning NMR of outer-membrane protein G from Escherichia coli., Chembiochem 6(9):1679-84
[7] Korkmaz F., Koster S., Yildiz O., Mantele W., 2008, The role of lipids for the functional integrity of porin: an FTIR study using lipid and protein reporter groups., Biochemistry 47(46):12126-34
[8] Koster S., van Pee K., Yildiz O., 2015, Purification, Refolding, and Crystallization of the Outer Membrane Protein OmpG from Escherichia coli., Methods Enzymol 557:149-66
[9] Misra R., Benson SA., 1989, A novel mutation, cog, which results in production of a new porin protein (OmpG) of Escherichia coli K-12., J Bacteriol 171(8):4105-11
[10] Thoma J., Manioglu S., Kalbermatter D., Bosshart PD., Fotiadis D., Muller DJ., 2018, Protein-enriched outer membrane vesicles as a native platform for outer membrane protein studies., Commun Biol 1:23

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