P0A7N4 (RL32_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L32

Gene names

Name:	rpmF
Ordered Locus Names:	b1089, JW1075

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	57 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Subunit structure	Part of the 50S ribosomal subunit. Contacts L17 (Ref.7).
Sequence similarities	Belongs to the ribosomal protein L32P family.
Mass spectrometry	Molecular mass is 6315.1 Da from positions 2 - 57. Determined by MALDI. Ref.8

Ontologies

Keywords
Molecular function	Ribonucleoprotein Ribosomal protein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: InterPro
Cellular component	large ribosomal subunit Inferred from electronic annotation. Source: InterPro
Molecular function	structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rpmB	P0A7M2	1	EBI-1112732,EBI-543024

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.5 Ref.6

Chain

2 – 57

56

50S ribosomal protein L32 HAMAP MF_00340

PRO_0000172338

Secondary structure

1

.

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.

.

.

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.

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.

.

57

Helix Strand Turn

Details...

Turn

9 – 15

7

Helix

16 – 20

5

Beta strand

31 – 35

5

Turn

38 – 41

4

Beta strand

44 – 46

3

Beta strand

49 – 55

7

Sequences

	Sequence		Length	Mass (Da)
	P0A7N4 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: FA07955DAA8E4E94	FASTA	57	6,446
	10 20 30 40 50 MAVQQNKPTR SKRGMRRSHD ALTAVTSLSV DKTSGEKHLR HHITADGYYR GRKVIAK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and analysis of an Escherichia coli operon containing the rpmF gene for ribosomal protein L32 and the gene for a 30-kilodalton protein." Tanaka Y., Tsujimura A., Fujita N., Isono S., Isono K. J. Bacteriol. 171:5707-5712(1989) [PubMed: 2477362] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The primary structure of protein L32 from the 50S subunit of Escherichia coli ribosomes." Wittmann-Liebold B., Greuer B., Pannenbecker R. Hoppe-Seyler's Z. Physiol. Chem. 356:1977-1979(1975) [PubMed: 765258] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-57. Strain: K.
[6]	"The primary structure of ribosomal protein L32 from E. coli MRE-600 ribosomes." Vinokurov L.M., Alakhov Y.B., Golov E.A., Ovchinnikov Y.A. Bioorg. Khim. 2:1013-1017(1976) Cited for: PROTEIN SEQUENCE OF 2-57. Strain: MRE-600.
[7]	"Comparative cross-linking study on the 50S ribosomal subunit from Escherichia coli." Walleczek J., Martin T., Redl B., Stoeffler-Meilicke M., Stoeffler G. Biochemistry 28:4099-4105(1989) [PubMed: 2665813] [Abstract] Cited for: CROSS-LINKING TO L17.
[8]	"Observation of Escherichia coli ribosomal proteins and their posttranslational modifications by mass spectrometry." Arnold R.J., Reilly J.P. Anal. Biochem. 269:105-112(1999) [PubMed: 10094780] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[9]	"Study of the structural dynamics of the E. coli 70S ribosome using real-space refinement." Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M., Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J. Cell 113:789-801(2003) [PubMed: 12809609] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[10]	"Structures of the bacterial ribosome at 3.5 A resolution." Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A., Holton J.M., Cate J.H.D. Science 310:827-834(2005) [PubMed: 16272117] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES. Strain: MRE-600.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M29698 Genomic DNA. Translation: AAA24575.1.
U00096 Genomic DNA. Translation: AAC74173.1.
AP009048 Genomic DNA. Translation: BAA35897.1.

PIR

R5EC32. JV0048.

RefSeq

NP_415607.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1P85	electron microscopy	12.30	Z	2-57	[»]
1P86	electron microscopy	11.50	Z	2-57	[»]
1VS6	X-ray	3.46	0	1-57	[»]
1VS8	X-ray	3.46	0	1-57	[»]
1VT2	X-ray	3.30	0	1-57	[»]
2AW4	X-ray	3.46	0	2-57	[»]
2AWB	X-ray	3.46	0	2-57	[»]
2GYA	electron microscopy	15.00	Z	28-55	[»]
2GYC	electron microscopy	15.00	Z	28-56	[»]
2I2T	X-ray	3.22	0	2-56	[»]
2I2V	X-ray	3.22	0	2-56	[»]
2J28	electron microscopy	8.00	0	2-56	[»]
2QAM	X-ray	3.21	0	2-57	[»]
2QAO	X-ray	3.21	0	2-57	[»]
2QBA	X-ray	3.54	0	2-57	[»]
2QBC	X-ray	3.54	0	2-57	[»]
2QBE	X-ray	3.30	0	2-57	[»]
2QBG	X-ray	3.30	0	2-57	[»]
2QBI	X-ray	4.00	0	2-57	[»]
2QBK	X-ray	4.00	0	2-57	[»]
2QOV	X-ray	3.93	0	2-57	[»]
2QOX	X-ray	3.93	0	2-57	[»]
2QOZ	X-ray	3.50	0	2-57	[»]
2QP1	X-ray	3.50	0	2-57	[»]
2RDO	electron microscopy	9.10	0	2-57	[»]
2WWQ	electron microscopy	5.80	3	2-57	[»]
2Z4L	X-ray	4.45	0	2-57	[»]
2Z4N	X-ray	4.45	0	2-57	[»]
3BBX	electron microscopy	10.00	0	2-57	[»]
3DF2	X-ray	3.50	0	2-56	[»]
3DF4	X-ray	3.50	0	2-56	[»]
3E1B	electron microscopy	-	T	1-57	[»]
3E1D	electron microscopy	-	T	1-57	[»]
3FIK	electron microscopy	6.70	0	2-57	[»]
3I1N	X-ray	3.19	0	1-57	[»]
3I1P	X-ray	3.19	0	1-57	[»]
3I1R	X-ray	3.81	0	1-57	[»]
3I1T	X-ray	3.81	0	1-57	[»]
3I20	X-ray	3.71	0	1-57	[»]
3I22	X-ray	3.71	0	1-57	[»]
3IZT	electron microscopy	-	c	1-57	[»]
3IZU	electron microscopy	-	c	1-57	[»]
3J01	electron microscopy	-	0	2-57	[»]
3KCR	electron microscopy	-	0	1-57	[»]
3OAS	X-ray	3.25	0	2-57	[»]
3OAT	X-ray	3.25	0	2-57	[»]
3OFC	X-ray	3.19	0	2-57	[»]
3OFD	X-ray	3.19	0	2-57	[»]
3OFQ	X-ray	3.10	0	2-57	[»]
3OFR	X-ray	3.10	0	2-57	[»]
3OFZ	X-ray	3.29	0	2-57	[»]
3OG0	X-ray	3.29	0	2-57	[»]
3ORB	X-ray	3.30	0	1-57	[»]
3R8S	X-ray	3.00	0	2-57	[»]
3R8T	X-ray	3.00	0	2-57	[»]

ProteinModelPortal

P0A7N4.

SMR

P0A7N4. Positions 2-57.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35782N.

IntAct

P0A7N4. 6 interactions.

2D gel databases

ECO2DBASE

I011.7. 6TH EDITION.

Proteomic databases

PRIDE

P0A7N4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000003897; EBESCP00000003897; EBESCG00000003186.
EBESCT00000003898; EBESCP00000003898; EBESCG00000003186.
EBESCT00000014717; EBESCP00000014008; EBESCG00000013778.

GeneID

945657.

GenomeReviews

Gene locus JW1075 in contig AP009048_GR.
Gene locus b1089 in contig U00096_GR.

KEGG

ecj:JW1075.
eco:b1089.

PATRIC

32117419. VBIEscCol129921_1132.

Organism-specific databases

EchoBASE

EB0883.

EcoGene

EG10890. rpmF.

Phylogenomic databases

eggNOG

COG0333.

GeneTree

EBGT00050000011513.

HOGENOM

HBG728381.

OMA

HRAHDFL.

PhylomeDB

P0A7N4.

ProtClustDB

PRK01110.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10890-MONOMER.

Gene expression databases

Genevestigator

P0A7N4.

Family and domain databases

HAMAP

MF_00340. Ribosomal_L32.
[Tree]

InterPro

IPR002677. Ribosomal_L32p.
IPR011332. Ribosomal_zn-bd_dom.
[Graphical view]

KO

K02911.

Pfam

PF01783. Ribosomal_L32p. 1 hit.
[Graphical view]

SUPFAM

SSF57829. Ribosomal_zn-bd. 1 hit.

TIGRFAMs

TIGR01031. RpmF_bact. 1 hit.

ProtoNet

Search...

Entry information

Entry name

RL32_ECOLI

Accession

Primary (citable) accession number: P0A7N4
Secondary accession number(s): P02435

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program