Outer membrane protein assembly factor BamC precursor

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P0A903 (BAMC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 76. History...

Clusters with 100%, 90%, 50% identity |

Documents (4) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Outer membrane protein assembly factor BamC

Gene names

Name:	bamC
Synonyms:	dapX, nlpB
Ordered Locus Names:	b2477, JW2462

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length	344 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. Ref.10 Ref.11 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 BamD and BamE. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11
Subcellular location	Cell outer membrane; Lipid-anchor Ref.7.
Domain	Contains two well-defined domains connected by a flexible linker. The C-terminal domain may serve as an important protein-binding surface for interaction with other Bam components or substrates. In addition, contains a long unstructured N-terminal region, which is required to stabilize the BamCD complex. Ref.14 Ref.16 Ref.17
Sequence similarities	Belongs to the BamC family.
Sequence caution	The sequence M33928 differs from that shown. Reason: Frameshift at positions 50, 64, 81 and 134.

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.10. Source: EcoCyc protein insertion into membrane Inferred from direct assay Ref.10. Source: EcoCyc
Cellular_component	cell outer membrane Inferred from direct assay Ref.7. Source: EcoCyc plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1129043,EBI-1129043
bamD	P0AC02	4	EBI-1129043,EBI-1128087

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 24

HAMAP-Rule MF_00924

Chain

25 – 344

320

Outer membrane protein assembly factor BamC HAMAP-Rule MF_00924

PRO_0000018027

Amino acid modifications

Lipidation

N-palmitoyl cysteine HAMAP-Rule MF_00924

Lipidation

S-diacylglycerol cysteine HAMAP-Rule MF_00924

Experimental info

Sequence conflict

219

A → R Ref.2

Secondary structure

344

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P0A903 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: 49991F277D9D923C
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FASTA

344

36,842

        10         20         30         40         50         60 
MAYSVQKSRL AKVAGVSLVL LLAACSSDSR YKRQVSGDEA YLEAAPLAEL HAPAGMILPV 

        70         80         90        100        110        120 
TSGDYAIPVT NGSGAVGKAL DIRPPAQPLA LVSGARTQFT GDTASLLVEN GRGNTLWPQV 

       130        140        150        160        170        180 
VSVLQAKNYT ITQRDDAGQT LTTDWVQWNR LDEDEQYRGR YQISVKPQGY QQAVTVKLLN 

       190        200        210        220        230        240 
LEQAGKPVAD AASMQRYSTE MMNVISAGLD KSATDAANAA QNRASTTMDV QSAADDTGLP 

       250        260        270        280        290        300 
MLVVRGPFNV VWQRLPAALE KVGMKVTDST RSQGNMAVTY KPLSDSDWQE LGASDPGLAS 

       310        320        330        340 
GDYKLQVGDL DNRSSLQFID PKGHTLTQSQ NDALVAVFQA AFSK

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A gene for a new lipoprotein in the dapA-purC interval of the Escherichia coli chromosome." Bouvier J., Pugsley A.P., Stragier P. J. Bacteriol. 173:5523-5531(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"DNA sequence of the purC gene encoding 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide synthetase and organization of the dapA-purC region of Escherichia coli K-12." Tiedemann A.A., Demarini D.J., Parker J., Smith J.M. J. Bacteriol. 172:6035-6041(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"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. 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.
[4]	"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.
[5]	"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.
[6]	"Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli." Wu T., Malinverni J., Ruiz N., Kim S., Silhavy T.J., Kahne D. Cell 121:235-245(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY. Strain: K12.
[7]	"Protein complexes of the Escherichia coli cell envelope." Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L., von Heijne G., Daley D.O. J. Biol. Chem. 280:34409-34419(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, SUBCELLULAR LOCATION. Strain: BL21-DE3.
[8]	"YfiO stabilizes the YaeT complex and is essential for outer membrane protein assembly in Escherichia coli." Malinverni J.C., Werner J., Kim S., Sklar J.G., Kahne D., Misra R., Silhavy T.J. Mol. Microbiol. 61:151-164(2006) [PubMed] [Europe PMC] [Abstract] Cited for: SUBUNIT, INTERACTION WITH BAMD. Strain: K12.
[9]	"Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli." Knowles T.J., McClelland D.M., Rajesh S., Henderson I.R., Overduin M. Biomol. NMR. Assign. 3:203-206(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SECONDARY STRUCTURE.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"Crystallographic analysis of the C-terminal domain of the Escherichia coli lipoprotein BamC." Kim K.H., Aulakh S., Tan W., Paetzel M. Acta Crystallogr. F 67:1350-1358(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 224-343, DOMAIN.
[15]	"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 (1.25 ANGSTROMS) OF 226-344.
[16]	"Crystal structure of beta-barrel assembly machinery BamCD protein complex." Kim K.H., Aulakh S., Paetzel M. J. Biol. Chem. 286:39116-39121(2011) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 26-344, INTERACTION WITH BAMD, DOMAIN. Strain: K12.
[17]	"Structure of the BamC two-domain protein obtained by Rosetta with a limited NMR data set." Warner L.R., Varga K., Lange O.F., Baker S.L., Baker D., Sousa M.C., Pardi A. J. Mol. Biol. 411:83-95(2011) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 101-344, DOMAIN.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X57402 Genomic DNA. Translation: CAA40661.1.
M33928 Genomic DNA. No translation available.
U00096 Genomic DNA. Translation: AAC75530.2.
AP009048 Genomic DNA. Translation: BAA16354.1.

PIR

D65023.

RefSeq

NP_416972.4. NC_000913.2.
YP_490705.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LAE	NMR	-	A	101-344	[»]
2LAF	NMR	-	A	101-344	[»]
2YH5	X-ray	1.25	A	226-344	[»]
2YH6	X-ray	1.55	A/B/C/D	101-212	[»]
3SNS	X-ray	1.50	A	224-343	[»]
3TGO	X-ray	2.90	C/D	26-344	[»]

ProteinModelPortal

P0A903.

SMR

P0A903. Positions 29-216, 226-344.

ModBase

Search...

Protein-protein interaction databases

IntAct

P0A903. 7 interactions.

STRING

511145.b2477.

Protein family/group databases

TCDB

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

2D gel databases

SWISS-2DPAGE

P0A903.

Proteomic databases

PaxDb

P0A903.

PRIDE

P0A903.

Protocols and materials databases

DNASU

946954.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC75530; AAC75530; b2477.
BAA16354; BAA16354; BAA16354.

GeneID

12933904.
946954.

KEGG

ecj:Y75_p2430.
eco:b2477.

PATRIC

32120341. VBIEscCol129921_2573.

Organism-specific databases

EchoBASE

EB0652.

EcoGene

EG10658. bamC.

Phylogenomic databases

eggNOG

COG3317.

HOGENOM

HOG000123040.

K07287.

OMA

NGDYKLQ.

ProtClustDB

PRK11679.

Enzyme and pathway databases

BioCyc

EcoCyc:EG10658-MONOMER.
ECOL316407:JW2462-MONOMER.

Gene expression databases

Genevestigator

P0A903.

Family and domain databases

HAMAP

MF_00924. OM_assembly_BamC.

InterPro

IPR014524. BamC.
IPR010653. Lipoprotein_NlpB.
[Graphical view]

Pfam

PF06804. Lipoprotein_18. 1 hit.
[Graphical view]

PIRSF

PIRSF026343. NlpB. 1 hit.

PROSITE

PS51257. PROKAR_LIPOPROTEIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0A903.

Entry information

Entry name

BAMC_ECOLI

Accession

Primary (citable) accession number: P0A903
Secondary accession number(s): P21167, P76564

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	May 1, 2013
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Recent format changes

Overview of recent format changes

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents