P0A937 (BAME_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Outer membrane protein assembly factor BamE

Gene names

Name:	bamE
Synonyms:	smpA
Ordered Locus Names:	b2617, JW2598

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	113 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)

Function	Part of the outer membrane protein assembly complex, which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Nonessential member of the complex that stabilizes the interaction between the essential proteins BamA and BamD. May modulate the conformation of BamA, likely through interactions with BamD. Ref.5 Ref.6 Ref.7 Ref.8 Ref.10 Ref.12
Subunit structure	Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. Forms a subcomplex with BamC and BamD. Monomer in the periplasm, but is able to adopt a dimeric conformation in the cytoplasm. Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Ref.11 Ref.12
Subcellular location	Cell outer membrane; Lipid-anchor Ref.5.
Disruption phenotype	Mutants show minor defects in the assembly of outer membrane proteins. Ref.5
Sequence similarities	Belongs to the BamE family.
Sequence caution	The sequence CAA36847.1 differs from that shown. Reason: Sequence of unknown provenance, it does not match this entry.

Ontologies

Keywords
Cellular component	Cell membrane Cell outer membrane Membrane
Domain	Signal
PTM	Lipoprotein Palmitate
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Gram-negative-bacterium-type cell outer membrane assembly Inferred from direct assay Ref.6. Source: EcoCyc protein insertion into membrane Inferred from direct assay Ref.6. Source: EcoCyc response to antibiotic Inferred from mutant phenotype Ref.5. Source: EcoCyc
Cellular_component	integral to cell outer membrane Inferred from genetic interaction Ref.5. Source: EcoliWiki plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		13	EBI-6391574,EBI-6391574

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

By similarity

Chain

20 – 113

94

Outer membrane protein assembly factor BamE HAMAP-Rule MF_00925

PRO_0000032810

Amino acid modifications

Lipidation

20

1

N-palmitoyl cysteine Probable

Lipidation

20

1

S-diacylglycerol cysteine Probable

Secondary structure

1

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113

Helix Strand Turn

Details...

Beta strand

35 – 37

3

Helix

40 – 43

4

Helix

52 – 59

8

Beta strand

63 – 65

3

Helix

67 – 69

3

Beta strand

71 – 76

6

Beta strand

85 – 87

3

Beta strand

90 – 95

6

Beta strand

99 – 107

9

Turn

109 – 112

4

Sequences

	Sequence		Length	Mass (Da)
	P0A937 [UniParc]. Last modified July 19, 2005. Version 1. Checksum: CFD8840C014AA0A2	FASTA	113	12,302
	10 20 30 40 50 60 MRCKTLTAAA AVLLMLTAGC STLERVVYRP DINQGNYLTA NDVSKIRVGM TQQQVAYALG 70 80 90 100 110 TPLMSDPFGT NTWFYVFRQQ PGHEGVTQQT LTLTFNSSGV LTNIDNKPAL SGN

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T. DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"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.
[3]	"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.
[4]	"Two new genes located between 2758 and 2761 kilobase pairs on the Escherichia coli genome." Chauhan A.K., Miczak A., Apirion D. J. Bacteriol. 173:3271-3272(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 64-113. Strain: K12.
[5]	"Lipoprotein SmpA is a component of the YaeT complex that assembles outer membrane proteins in Escherichia coli." Sklar J.G., Wu T., Gronenberg L.S., Malinverni J.C., Kahne D., Silhavy T.J. Proc. Natl. Acad. Sci. U.S.A. 104:6400-6405(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. Strain: K12.
[6]	"Reconstitution of outer membrane protein assembly from purified components." Hagan C.L., Kim S., Kahne D. Science 328:890-892(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[7]	"The reconstituted Escherichia coli Bam complex catalyzes multiple rounds of beta-barrel assembly." Hagan C.L., Kahne D. Biochemistry 50:7444-7446(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[8]	"BamE modulates the Escherichia coli beta-barrel assembly machine component BamA." Rigel N.W., Schwalm J., Ricci D.P., Silhavy T.J. J. Bacteriol. 194:1002-1008(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[9]	"Crystallization and preliminary X-ray data collection of the Escherichia coli lipoproteins BamC, BamD and BamE." Albrecht R., Zeth K. Acta Crystallogr. F 66:1586-1590(2010) [PubMed] [Europe PMC] [Abstract] Cited for: CRYSTALLIZATION, SUBUNIT.
[10]	"Structural characterization of Escherichia coli BamE, a lipoprotein component of the beta-barrel assembly machinery complex." Kim K.H., Kang H.S., Okon M., Escobar-Cabrera E., McIntosh L.P., Paetzel M. Biochemistry 50:1081-1090(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 21-113, FUNCTION, SUBUNIT.
[11]	"Structure and function of BamE within the outer membrane and the beta-barrel assembly machine." Knowles T.J., Browning D.F., Jeeves M., Maderbocus R., Rajesh S., Sridhar P., Manoli E., Emery D., Sommer U., Spencer A., Leyton D.L., Squire D., Chaudhuri R.R., Viant M.R., Cunningham A.F., Henderson I.R., Overduin M. EMBO Rep. 12:123-128(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 21-113, SUBUNIT.
[12]	"Structural basis of outer membrane protein biogenesis in bacteria." Albrecht R., Zeth K. J. Biol. Chem. 286:27792-27803(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 34-113, SUBUNIT, FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U36840 Genomic DNA. Translation: AAA79787.1.
U00096 Genomic DNA. Translation: AAC75666.2.
AP009048 Genomic DNA. Translation: BAA16502.1.
X52620 Genomic DNA. Translation: CAA36847.1. Sequence problems.

PIR

S11646.
T08630.

RefSeq

NP_417107.2. NC_000913.2.
YP_490839.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KM7	NMR	-	A	21-113	[»]
2KXX	NMR	-	A	21-113	[»]
2YH9	X-ray	1.80	A/B/C	34-113	[»]

ProteinModelPortal

P0A937.

SMR

P0A937. Positions 21-113.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A937. 1 interaction.

STRING

511145.b2617.

Protein family/group databases

TCDB

1.B.33.1.3. outer membrane protein insertion porin (Bam Complex) (OmpIP) family.

Proteomic databases

PRIDE

P0A937.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75666; AAC75666; b2617.
BAA16502; BAA16502; BAA16502.

GeneID

12930576.
945583.

KEGG

ecj:Y75_p2564.
eco:b2617.

PATRIC

32120633. VBIEscCol129921_2715.

Organism-specific databases

EchoBASE

EB0945.

EcoGene

EG10952. bamE.

Phylogenomic databases

eggNOG

COG2913.

HOGENOM

HOG000256181.

KO

K06186.

OMA

NTWYYIY.

ProtClustDB

PRK11548.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10952-MONOMER.
ECOL316407:JW2598-MONOMER.

Gene expression databases

Genevestigator

P0A937.

Family and domain databases

HAMAP

MF_00925. OM_assembly_BamE.

InterPro

IPR026592. BamE.
IPR007450. Lipoprotein_SmpA/OmlA.
[Graphical view]

Pfam

PF04355. SmpA_OmlA. 1 hit.
[Graphical view]

PROSITE

PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A937.

Entry information

Entry name

BAME_ECOLI

Accession

Primary (citable) accession number: P0A937
Secondary accession number(s): P23089

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program