P0A7M6 (RL29_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
50S ribosomal protein L29

Gene names

Name:	rpmC
Ordered Locus Names:	b3312, JW3274

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	63 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binds 23S rRNA. It is not essential for growth. HAMAP-Rule MF_00374 One of the proteins that surrounds the polypeptide exit tunnel on the outside of the subunit. Contacts trigger factor (Ref.9). HAMAP-Rule MF_00374
Subunit structure	Part of the 50s ribosomal subunit. Contacts protein L23 (Ref.7), trigger factor (Ref.9) and protein nascent chains (Ref.10). Might also contact SecE and probably does contact SecG when the SecYEG translocation complex is docked with the ribosome.
Disruption phenotype	Cells missing both S17 and L29 grow very slowly and have a rather unstable temperature-sensitive phenotype. Ref.9
Sequence similarities	Belongs to the ribosomal protein L29P family.
Mass spectrometry	Molecular mass is 7273.4 Da from positions 1 - 63. Determined by MALDI. Ref.11
Sequence caution	The sequence described in Ref.1 differs from that shown. Reason: Exchange of two tryptic peptides.

Ontologies

Keywords
Ligand	RNA-binding rRNA-binding
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: HAMAP
Cellular_component	ribosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	rRNA binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of ribosome Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 63

63

50S ribosomal protein L29 HAMAP-Rule MF_00374

PRO_0000130384

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

63

Helix Strand Turn

Details...

Helix

3 – 5

3

Beta strand

6 – 8

3

Helix

10 – 21

12

Helix

23 – 33

11

Beta strand

37 – 39

3

Helix

40 – 42

3

Helix

44 – 55

12

Turn

56 – 58

3

Turn

59 – 62

4

Sequences

	Sequence		Length	Mass (Da)
	P0A7M6 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: DAEF8F126B0AA077	FASTA	63	7,273
	10 20 30 40 50 60 MKAKELREKS VEELNTELLN LLREQFNLRM QAASGQLQQS HLLKQVRRDV ARVKTLLNEK AGA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The primary structure of the ribosomal protein L29 from Escherichia coli." Bitar K.G. Biochim. Biophys. Acta 386:99-106(1975) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE. Strain: K.
[2]	"Structure of the Escherichia coli S10 ribosomal protein operon." Zurawski G., Zurawski S.M. Nucleic Acids Res. 13:4521-4526(1985) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"The use of 2-iminothiolane as an RNA-protein cross-linking agent in Escherichia coli ribosomes, and the localisation on 23S RNA of sites cross-linked to proteins L4, L6, L21, L23, L27 and L29." Wower I., Wower J., Meinke M., Brimacombe R. Nucleic Acids Res. 9:4285-4302(1981) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO 23S RRNA. Strain: MRE-600.
[6]	"A mutant from Escherichia coli which lacks ribosomal proteins S17 and L29 used to localize these two proteins on the ribosomal surface." Stoeffler-Meilicke M., Dabbs E.R., Albrecht-Ehrlich R., Stoeffler G. Eur. J. Biochem. 150:485-490(1985) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF A STRAIN MISSING S17 AND L29. Strain: AM111.
[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] [Europe PMC] [Abstract] Cited for: CROSS-LINKING TO L23.
[8]	"Escherichia coli proteome analysis using the gene-protein database." VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C. Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY 2D-GEL.
[9]	"L23 protein functions as a chaperone docking site on the ribosome." Kramer G., Rauch T., Rist W., Vorderwuelbecke S., Patzelt H., Schulze-Specking A., Ban N., Deuerling E., Bukau B. Nature 419:171-174(2002) [PubMed] [Europe PMC] [Abstract] Cited for: BINDING TO TRIGGER FACTOR, DISRUPTION PHENOTYPE. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[10]	"Interplay of signal recognition particle and trigger factor at L23 near the nascent chain exit site on the Escherichia coli ribosome." Ullers R.S., Houben E.N.G., Raine A., ten Hagen-Jongman C.M., Ehrenberg M., Brunner J., Oudega B., Harms N., Luirink J. J. Cell Biol. 161:679-684(2003) [PubMed] [Europe PMC] [Abstract] Cited for: CROSS-LINKS TO NASCENT PROTEIN CHAINS. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[11]	"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] [Europe PMC] [Abstract] Cited for: MASS SPECTROMETRY. Strain: K12 / ATCC 25404 / DSM 5698 / NCIMB 11290.
[12]	"Structure of the E. coli protein-conducting channel bound to a translating ribosome." Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III, Ban N., Frank J. Nature 438:318-324(2005) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE CONTACT WITH THE SECYEG TRANSLOCATION COMPLEX. Strain: MRE-600.
[13]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS). Strain: MRE-600.
[14]	"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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES. Strain: MRE-600.
[15]	"Cryo-EM structure of the ribosome-SecYE complex in the membrane environment." Frauenfeld J., Gumbart J., Sluis E.O., Funes S., Gartmann M., Beatrix B., Mielke T., Berninghausen O., Becker T., Schulten K., Beckmann R. Nat. Struct. Mol. Biol. 18:614-621(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY CRYOELECTRON MICROSCOPY IN COMPLEX WITH SECYE AND A NASCENT POLYPEPTIDE CHAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X02613 Genomic DNA. Translation: CAA26468.1.
U18997 Genomic DNA. Translation: AAA58109.1.
U00096 Genomic DNA. Translation: AAC76337.1.
AP009048 Genomic DNA. Translation: BAE77979.1.

PIR

R5EC29. B37519.

RefSeq

NP_417771.1. NC_000913.2.
YP_492120.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ML5	electron microscopy	14.00	w	2-63	[»]
1P85	electron microscopy	12.30	W	1-63	[»]
1P86	electron microscopy	11.50	W	1-63	[»]
1VS6	X-ray	3.46	X	1-63	[»]
1VS8	X-ray	3.46	X	1-63	[»]
1VT2	X-ray	3.30	Y	1-63	[»]
2AW4	X-ray	3.46	X	1-63	[»]
2AWB	X-ray	3.46	X	1-63	[»]
2GYA	electron microscopy	15.00	W	1-60	[»]
2GYC	electron microscopy	15.00	W	1-60	[»]
2I2T	X-ray	3.22	Y	1-63	[»]
2I2V	X-ray	3.22	Y	1-63	[»]
2J28	electron microscopy	8.00	X	1-63	[»]
2QAM	X-ray	3.21	X	1-63	[»]
2QAO	X-ray	3.21	X	1-63	[»]
2QBA	X-ray	3.54	X	1-63	[»]
2QBC	X-ray	3.54	X	1-63	[»]
2QBE	X-ray	3.30	X	1-63	[»]
2QBG	X-ray	3.30	X	1-63	[»]
2QBI	X-ray	4.00	X	1-63	[»]
2QBK	X-ray	4.00	X	1-63	[»]
2QOV	X-ray	3.93	X	1-63	[»]
2QOX	X-ray	3.93	X	1-63	[»]
2QOZ	X-ray	3.50	X	1-63	[»]
2QP1	X-ray	3.50	X	1-63	[»]
2RDO	electron microscopy	9.10	X	1-63	[»]
2VHM	X-ray	3.74	X	1-63	[»]
2VHN	X-ray	3.74	X	1-63	[»]
2VRH	electron microscopy	19.00	D	1-63	[»]
2WWQ	electron microscopy	5.80	1	1-63	[»]
2Z4L	X-ray	4.45	X	1-63	[»]
2Z4N	X-ray	4.45	X	1-63	[»]
3BBX	electron microscopy	10.00	X	1-63	[»]
3DF2	X-ray	3.50	X	1-63	[»]
3DF4	X-ray	3.50	X	1-63	[»]
3E1B	electron microscopy	-	Q	1-63	[»]
3E1D	electron microscopy	-	Q	1-63	[»]
3FIK	electron microscopy	6.70	Y	1-63	[»]
3I1N	X-ray	3.19	Y	1-63	[»]
3I1P	X-ray	3.19	Y	1-63	[»]
3I1R	X-ray	3.81	Y	1-63	[»]
3I1T	X-ray	3.81	Y	1-63	[»]
3I20	X-ray	3.71	Y	1-63	[»]
3I22	X-ray	3.71	Y	1-63	[»]
3IZT	electron microscopy	-	Z	1-63	[»]
3IZU	electron microscopy	-	Z	1-63	[»]
3J01	electron microscopy	-	Y	1-63	[»]
3J0T	electron microscopy	12.10	0	1-63	[»]
3J0W	electron microscopy	14.70	0	1-63	[»]
3J0Y	electron microscopy	13.50	0	1-63	[»]
3J11	electron microscopy	13.10	0	1-63	[»]
3J12	electron microscopy	11.50	0	1-63	[»]
3J14	electron microscopy	11.50	0	1-63	[»]
3J19	electron microscopy	8.30	Y	1-63	[»]
3KCR	electron microscopy	-	Y	1-63	[»]
3OAS	X-ray	3.25	Y	1-63	[»]
3OAT	X-ray	3.25	Y	1-63	[»]
3OFC	X-ray	3.19	Y	1-63	[»]
3OFD	X-ray	3.19	Y	1-63	[»]
3OFQ	X-ray	3.10	Y	1-63	[»]
3OFR	X-ray	3.10	Y	1-63	[»]
3OFZ	X-ray	3.29	Y	1-63	[»]
3OG0	X-ray	3.29	Y	1-63	[»]
3ORB	X-ray	3.30	Y	1-63	[»]
3R8S	X-ray	3.00	Y	1-63	[»]
3R8T	X-ray	3.00	Y	1-63	[»]
3SGF	X-ray	3.20	2	1-63	[»]
3UOS	X-ray	3.70	2	1-63	[»]
4GAR	X-ray	3.30	Y	1-63	[»]
4GAU	X-ray	3.30	Y	1-63	[»]

ProteinModelPortal

P0A7M6.

SMR

P0A7M6. Positions 1-63.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-47911N.

IntAct

P0A7M6. 33 interactions.

MINT

MINT-1240640.

STRING

511145.b3312.

Proteomic databases

PaxDb

P0A7M6.

PRIDE

P0A7M6.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC76337; AAC76337; b3312.
BAE77979; BAE77979; BAE77979.

GeneID

12934441.
947807.

KEGG

ecj:Y75_p3864.
eco:b3312.

PATRIC

32122056. VBIEscCol129921_3405.

Organism-specific databases

EchoBASE

EB0880.

EcoGene

EG10887. rpmC.

Phylogenomic databases

eggNOG

COG0255.

HOGENOM

HOG000248754.

KO

K02904.

OMA

QLAQTHT.

ProtClustDB

PRK00306.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10887-MONOMER.
ECOL316407:JW3274-MONOMER.

Gene expression databases

Genevestigator

P0A7M6.

Family and domain databases

Gene3D

1.10.287.310. 1 hit.

HAMAP

MF_00374. Ribosomal_L29.

InterPro

IPR001854. Ribosomal_L29.
IPR018254. Ribosomal_L29_CS.
[Graphical view]

Pfam

PF00831. Ribosomal_L29. 1 hit.
[Graphical view]

SUPFAM

SSF46561. Ribosomal_L29. 1 hit.

TIGRFAMs

TIGR00012. L29. 1 hit.

PROSITE

PS00579. RIBOSOMAL_L29. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A7M6.

Entry information

Entry name

RL29_ECOLI

Accession

Primary (citable) accession number: P0A7M6
Secondary accession number(s): P02429, Q2M6X7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	May 1, 2013
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program