RegulonDB

Gene
Name:	rpmF
Synonym(s):	ECK1075, EG10890, b1089
Genome position(nucleotides):	1147367 --> 1147540 Genome Browser
Strand:	forward
Sequence:	Get nucleotide sequence FastaFormat
GC content %:	54.02
External database links:

ASAP:	ABE-0003686
CGSC:	17605
ECHOBASE:	EB0883
ECOLIHUB:	rpmF
OU-MICROARRAY:	b1089
STRING:	511145.b1089
COLOMBOS:	rpmF

Product

Name:

50S ribosomal subunit protein L32

Synonym(s):

RpmF

Sequence:

Get amino acid sequence Fasta Format

Cellular location:

ribosome,cytosol

Molecular weight:

6.446

Isoelectric point:

11.623

Motif(s):

Type	Positions	Sequence
	2 -> 57	AVQQNKPTRSKRGMRRSHDALTAVTSLSVDKTSGEKHLRHHITADGYYRGRKVIAK

Classification:

Multifun Terms (GenProtEC)
		2 - information transfer --> 2.3 - protein related --> 2.3.2 - translation
		2 - information transfer --> 2.3 - protein related --> 2.3.8 - ribosomal proteins
		6 - cell structure --> 6.6 - ribosomes
Gene Ontology Terms (GO)
	cellular_component	GO:0005829 - cytosol GO:0005840 - ribosome GO:0015934 - large ribosomal subunit GO:0022625 - cytosolic large ribosomal subunit
	molecular_function	GO:0003735 - structural constituent of ribosome GO:0005515 - protein binding
	biological_process	GO:0006412 - translation GO:0000027 - ribosomal large subunit assembly GO:0000302 - response to reactive oxygen species GO:0009314 - response to radiation

Note(s):

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

Reference(s):

[1] Andrieux E., et al., 1984
[2] Barritault D., et al., 1975
[3] Bausk EV., et al., 1985
[4] Dzionara M., et al., 1977
[5] Gimautdinova OI., et al., 1981
[6] Gimautdinova OI., et al., 1982
[7] Gimautdinova OI., et al., 1984
[8] Graifer DM., et al., 1989
[9] Isono S., et al., 1978
[10] Janda I., et al., 1985
[11] Laughrea M., et al., 1987
[12] Mustoe AM., et al., 2018
[13] Oh W., et al., 1992
[14] Pichon JL., et al., 1977
[15] Podkovyrov S., et al., 1995
[16] Tanaka Y., et al., 1989
[17] Tejedor F., et al., 1985
[18] Wittmann-Liebold B., et al., 1975
[19] Zhang Y., et al., 1998

External database links:

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REFSEQ:

SMR:

UNIPROT:

Operon

Name:

yceD-rpmF-plsX-fabHDG-acpP-fabF

Operon arrangement:

Transcription unit	Promoter
yceD-rpmF	yceDp1
yceD-rpmF	yceDp2
rpmF-plsX-fabHDG	rpmFp
plsX-fabHDG	plsXp
fabHDG	fabHp
acpP	acpPp
acpP-fabF	acpPp
fabDG-acpP
fabF
fabG-acpP

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

Type	Name	Post Left	Strand	Notes	Evidence (Confirmed, Strong, Weak)	References
promoter	TSS_1370	1146794	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1371	1146809	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1372	1147056	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1373	1147094	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1374	1147132	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1375 (cluster)	1147141	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1376 (cluster)	1147146	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1377	1147188	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1378	1147194	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1379 (cluster)	1147206	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1380	1147213	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1381	1147215	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1382 (cluster)	1147300	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1383	1147307	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1384 (cluster)	1147313	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1385	1147350	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1386 (cluster)	1147395	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1387	1147771	forward	nd	[RS-EPT-CBR]	[20]
promoter	TSS_1388	1148362	forward	nd	[RS-EPT-CBR]	[20]

Evidence
[RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates

Reference(s)
[1] Andrieux E., Cozzone AJ., 1984, Conformational changes in bacterial polysomes induced by amino acid starvation., Int J Biochem 16(1):113-6
[2] Barritault D., Expert-Bezancon A., Milet M., 1975, [Nearest-neighbor relationships among 50S ribosomal proteins of E. coli]., C R Acad Sci Hebd Seances Acad Sci D 281(14):1043-6
[3] Bausk EV., Graifer DM., Karpova GG., 1985, [Study of the photoaffinity modification of Escherichia coli ribosomes near the donor tRNA-binding center]., Mol Biol (Mosk) 19(2):545-52
[4] Dzionara M., Robinson SM., Wittmann-Liebold B., 1977, Prediction for secondary structures of ten proteins from the 50S subunit of the Escherichia coli ribosome., J Supramol Struct 7(2):191-204
[5] Gimautdinova OI., Karpova GG., Knorre DG., Kobetz ND., 1981, The proteins of the messenger RNA binding site of Escherichia coli ribosomes., Nucleic Acids Res 9(14):3465-81
[6] Gimautdinova OI., Karpova GG., Kozyreva NA., 1982, [Affinity labeling of ribosomes from Escherichia coli with 4-(N-2-chloroethyl-N-methylamino) benzyl-5'-phosphamides of oligouridylates of different length]., Mol Biol (Mosk) 16(4):752-62
[7] Gimautdinova OI., Zenkova MA., Karpova GG., Podust LM., 1984, [Affinity modification of Escherichia coli ribosomes with photoactivated analogs of mRNA]., Mol Biol (Mosk) 18(4):907-18
[8] Graifer DM., Babkina GT., Matasova NB., Vladimirov SN., Karpova GG., Vlassov VV., 1989, Structural arrangement of tRNA binding sites on Escherichia coli ribosomes, as revealed from data on affinity labelling with photoactivatable tRNA derivatives., Biochim Biophys Acta 1008(2):146-56
[9] Isono S., Isono K., 1978, Mutations affecting the structural genes and the genes coding for modifying enzymes for ribosomal proteins in Escherichia coli., Mol Gen Genet 165(1):15-20
[10] Janda I., Kitakawa M., Isono K., 1985, Gene rpmF for ribosomal protein L32 and gene rimJ for a ribosomal protein acetylating enzyme are located near pyrC (23.4 min) in Escherichia coli., Mol Gen Genet 201(3):433-6
[11] Laughrea M., Latulippe J., Filion AM., Boulet L., 1987, Mistranslation in twelve Escherichia coli ribosomal proteins. Cysteine misincorporation at neutral amino acid residues other than tryptophan., Eur J Biochem 169(1):59-64
[12] Mustoe AM., Busan S., Rice GM., Hajdin CE., Peterson BK., Ruda VM., Kubica N., Nutiu R., Baryza JL., Weeks KM., 2018, Pervasive Regulatory Functions of mRNA Structure Revealed by High-Resolution SHAPE Probing., Cell 173(1):181-195.e18
[13] Oh W., Larson TJ., 1992, Physical locations of genes in the rne (ams)-rpmF-plsX-fab region of the Escherichia coli K-12 chromosome., J Bacteriol 174(23):7873-4
[14] Pichon JL., Coeroli C., Marchis-Mouren G., 1977, Studies on ribosomal protein biosynthesis in an RNA polymerase temperature sensitive E. coli mutant., Mol Gen Genet 150(3):257-64
[15] Podkovyrov S., Larson TJ., 1995, Lipid biosynthetic genes and a ribosomal protein gene are cotranscribed., FEBS Lett 368(3):429-31
[16] Tanaka Y., Tsujimura A., Fujita N., Isono S., Isono K., 1989, Cloning and analysis of an Escherichia coli operon containing the rpmF gene for ribosomal protein L32 and the gene for a 30-kilodalton protein., J Bacteriol 171(10):5707-12
[17] Tejedor F., Ballesta JP., 1985, Ribosome structure: binding site of macrolides studied by photoaffinity labeling., Biochemistry 24(2):467-72
[18] Wittmann-Liebold B., Greuer B., Pannenbecker R., 1975, The primary structure of protein L32 from the 50S subunit of Escherichia coli ribosomes., Hoppe Seylers Z Physiol Chem 356(12):1977-9
[19] Zhang Y., Cronan JE., 1998, Transcriptional analysis of essential genes of the Escherichia coli fatty acid biosynthesis gene cluster by functional replacement with the analogous Salmonella typhimurium gene cluster., J Bacteriol 180(13):3295-303
[20] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.