UniProtKB - P0AC02 (BAMD_ECOLI)

BLAST

>sp|P0AC02|BAMD_ECOLI Outer membrane protein assembly factor BamD OS=Escherichia coli (strain K12) OX=83333 GN=bamD PE=1 SV=1
MTRMKYLVAAATLSLFLAGCSGSKEEVPDNPPNEIYATAQQKLQDGNWRQAITQLEALDN
RYPFGPYSQQVQLDLIYAYYKNADLPLAQAAIDRFIRLNPTHPNIDYVMYMRGLTNMALD
DSALQGFFGVDRSDRDPQHARAAFSDFSKLVRGYPNSQYTTDATKRLVFLKDRLAKYEYS
VAEYYTERGAWVAVVNRVEGMLRDYPDTQATRDALPLMENAYRQMQMNAQAEKVAKIIAA
NSSNT

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History
Entry version 106 (07 Nov 2018)
Sequence version 1 (08 Nov 2005)
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Protein

Outer membrane protein assembly factor BamD

Gene

bamD

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamA, the core component of the assembly machinery. Probably involved in transient protein interactions. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits (PubMed:20378773, PubMed:21823654, PubMed:27686148). A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).9 Publications

GO - Biological processⁱ

View the complete GO annotation on QuickGO ...

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7352-MONOMER

BioCycⁱ

EcoCyc:G7352-MONOMER

Protein family/group databases

TCDBⁱ	1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

TCDBⁱ

1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Outer membrane protein assembly factor BamDUniRule annotation
Gene namesⁱ	Name:bamDUniRule annotation Synonyms:yfiO Ordered Locus Names:b2595, JW2577
Organismⁱ	Escherichia coli (strain K12)
Taxonomic identifierⁱ	83333 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli
Proteomesⁱ	UP000000318 Componentⁱ: Chromosome UP000000625 Componentⁱ: Chromosome

Organism-specific databases

EcoGeneⁱ	EG14222 bamD

EcoGeneⁱ

EG14222 bamD

Subcellular locationⁱ

Cell outer membrane
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00922
3 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "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.
- Ref.15
  "Structure of the BAM complex and its implications for biogenesis of outer-membrane proteins."
  Han L., Zheng J., Wang Y., Yang X., Liu Y., Sun C., Cao B., Zhou H., Ni D., Lou J., Zhao Y., Huang Y.
  Nat. Struct. Mol. Biol. 23:192-196(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (3.56 ANGSTROMS) OF 20-245 IN LATERAL CLOSED BAM COMPLEX, SUBUNIT, SUBCELLULAR LOCATION.
- Ref.16
  "Structural basis of outer membrane protein insertion by the BAM complex."
  Gu Y., Li H., Dong H., Zeng Y., Zhang Z., Paterson N.G., Stansfeld P.J., Wang Z., Zhang Y., Wang W., Dong C.
  Nature 531:64-69(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN LATERAL CLOSED BAM COMPLEX AND LATERAL OPEN BAMACDE SUBCOMPLEX, SUBUNIT, SUBCELLULAR LOCATION.
; Lipid-anchor
UniRule annotation
Manual assertion according to rulesⁱ
- HAMAP-Rule:MF_00922
2 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "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.
- Ref.14
  "Lateral opening in the intact beta-barrel assembly machinery captured by cryo-EM."
  Iadanza M.G., Higgins A.J., Schiffrin B., Calabrese A.N., Brockwell D.J., Ashcroft A.E., Radford S.E., Ranson N.A.
  Nat. Commun. 7:12865-12865(2016) [PubMed] [Europe PMC] [Abstract]
  Cited for: STRUCTURE BY ELECTRON MICROSCOPY (4.90 ANGSTROMS) OF 26-243 IN LATERAL OPEN BAM COMPLEX, FUNCTION, SUBUNIT, MASS SPECTROMETRY, DIACYLGLYCEROL AT CYS-20, PALMITOYLATION AT CYS-20.

GO - Cellular componentⁱ

Bam protein complex
Source: EcoCyc
Inferred from direct assayⁱ

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell outer membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Depletion decreases the density of outer membrane proteins, but does not significantly affect transport of lipopolysaccharides to the outer membrane.1 Publication

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Signal peptideⁱ	1 – 19	UniRule annotationAdd BLAST		19
ChainⁱPRO_0000036226	20 – 245	Outer membrane protein assembly factor BamDAdd BLAST		226

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Lipidationⁱ	20	N-palmitoyl cysteine1 Publication		1
Lipidationⁱ	20	S-diacylglycerol cysteine1 Publication		1

Keywords - PTMⁱ

Lipoprotein, Palmitate

Proteomic databases

EPDⁱ	P0AC02
PaxDbⁱ	P0AC02
PRIDEⁱ	P0AC02

Interactionⁱ

Subunit structureⁱ

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 BamE. Interacts directly with BamA. The Bam complex has the shape of a hat, with the BamA beta-barrel crown in the outer membrane and the periplasmic brim formed by the BamA POTRA domains and the 4 lipoproteins (PubMed:27686148, PubMed:26900875, PubMed:26901871, PubMed:26744406).12 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
atoA	P76459	2	EBI-1128087,EBI-1128061
bamA	P0A940	26	EBI-1128087,EBI-907371
bamC	P0A903	4	EBI-1128087,EBI-1129043
bamE	P0A937	3	EBI-1128087,EBI-6391574

Protein-protein interaction databases

BioGridⁱ	4260615, 311 interactors 851422, 1 interactor
ComplexPortalⁱ	CPX-1923 Bam complex
Database of interacting proteins More...DIPⁱ	DIP-51120N
IntActⁱ	P0AC02, 6 interactors
Molecular INTeraction database More...MINTⁱ	P0AC02
STRINGⁱ	316385.ECDH10B_2763

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	32 – 45	Combined sources	14
Helixⁱ	48 – 61	Combined sources	14
Helixⁱ	68 – 81	Combined sources	14
Helixⁱ	85 – 98	Combined sources	14
Beta strandⁱ	100 – 102	Combined sources	3
Helixⁱ	105 – 120	Combined sources	16
Turnⁱ	126 – 129	Combined sources	4
Beta strandⁱ	133 – 135	Combined sources	3
Helixⁱ	138 – 151	Combined sources	14
Helixⁱ	160 – 188	Combined sources	29
Helixⁱ	191 – 204	Combined sources	14
Helixⁱ	209 – 224	Combined sources	16
Helixⁱ	228 – 240	Combined sources	13

Show more details

3D structure databases

ProteinModelPortalⁱ	P0AC02
SMRⁱ	P0AC02
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domainⁱ

The N-terminal may interact with various proteins as a chaperone to assist in the folding and insertion of proteins into the outer membrane. The C-terminal region may serve as the link between BamA, BamC and BamE.1 Publication

Sequence similaritiesⁱ

Belongs to the BamD family.UniRule annotation

Keywords - Domainⁱ

Signal

Phylogenomic databases

eggNOGⁱ	ENOG4106SNF Bacteria COG4105 LUCA
HOGENOMⁱ	HOG000260923
InParanoidⁱ	P0AC02
KEGG Orthology (KO) More...KOⁱ	K05807
PhylomeDBⁱ	P0AC02

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd15830 BamD, 1 hit
Gene3Dⁱ	1.25.40.10, 1 hit
HAMAPⁱ	MF_00922 OM_assembly_BamD, 1 hit
InterProⁱ	View protein in InterPro IPR017689 BamD IPR039565 BamD-like IPR011990 TPR-like_helical_dom_sf
PANTHERⁱ	PTHR37423 PTHR37423, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF13525 YfiO, 1 hit
SUPFAMⁱ	SSF48452 SSF48452, 1 hit
TIGRFAMsⁱ	TIGR03302 OM_YfiO, 1 hit
PROSITEⁱ	View protein in PROSITE PS51257 PROKAR_LIPOPROTEIN, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

P0AC02-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MTRMKYLVAA ATLSLFLAGC SGSKEEVPDN PPNEIYATAQ QKLQDGNWRQ 
        60         70         80         90        100
AITQLEALDN RYPFGPYSQQ VQLDLIYAYY KNADLPLAQA AIDRFIRLNP 
       110        120        130        140        150
THPNIDYVMY MRGLTNMALD DSALQGFFGV DRSDRDPQHA RAAFSDFSKL 
       160        170        180        190        200
VRGYPNSQYT TDATKRLVFL KDRLAKYEYS VAEYYTERGA WVAVVNRVEG 
       210        220        230        240 
MLRDYPDTQA TRDALPLMEN AYRQMQMNAQ AEKVAKIIAA NSSNT

Length:245

Mass (Da):27,829

Last modified:November 8, 2005 - v1

Checksum:ⁱ91D0A25E69248C49

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	59	D → Y in CAA94434 (Ref. 4) Curated		1

Mass spectrometryⁱ

Molecular mass is 26582 Da from positions 20 - 245. Determined by ESI. With 3 palmitic acid (C16) acyl chains.1 Publication

Molecular mass is 26603 Da from positions 20 - 245. Determined by ESI. With 2 palmitic (C16) and 1 stearic (C18) acid acyl chains.1 Publication

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC75644.1 AP009048 Genomic DNA Translation: BAA16480.1 Z70523 Genomic DNA Translation: CAA94434.1
PIRⁱ	F65037
NCBI Reference Sequences More...RefSeqⁱ	NP_417086.1, NC_000913.3 WP_000197686.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC75644; AAC75644; b2595 BAA16480; BAA16480; BAA16480
GeneIDⁱ	947086
KEGGⁱ	ecj:JW2577 eco:b2595
PATRICⁱ	fig\|1411691.4.peg.4142

Protein	Similar proteins		Species	Score	Length	Source
P0AC02	Outer membrane protein assembly factor BamD		ECO57		245	UniRef100_P0AC04
Outer membrane protein assembly factor BamD		ECOL6		245
YfiO domain containing protein		TRITR		245
Outer membrane protein assembly factor BamD		Shigella sp.		245
Outer membrane protein assembly factor BamD		Escherichia coli O145 str. RM9872		245
+171

Protein	Similar proteins		Species	Score	Length	Source
P0AC02	Outer membrane protein assembly factor BamD		ECO57		245	UniRef90_P0AC04
Outer membrane protein assembly factor BamD		ECOL6		245
YfiO domain containing protein		TRITR		245
Outer membrane protein assembly factor BamD		Shigella sp.		245
Outer membrane protein assembly factor BamD		Escherichia coli O145 str. RM9872		245
+823

Protein	Similar proteins		Species	Score	Length	Source
P0AC02	Outer membrane protein assembly factor BamD		ECO57		245	UniRef50_P0AC04
Outer membrane protein assembly factor BamD		ECOL6		245
YfiO domain containing protein		TRITR		245
Outer membrane protein assembly factor BamD		Shigella sp.		245
Outer membrane protein assembly factor BamD		Escherichia coli O145 str. RM9872		245
+1518

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U00096 Genomic DNA Translation: AAC75644.1 AP009048 Genomic DNA Translation: BAA16480.1 Z70523 Genomic DNA Translation: CAA94434.1
PIRⁱ	F65037
RefSeqⁱ	NP_417086.1, NC_000913.3 WP_000197686.1, NZ_LN832404.1

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	2YHC	X-ray	1.80	A	29-245	[»]
	3Q5M	X-ray	2.60	A	23-245	[»]
	3TGO	X-ray	2.90	A/B	21-245	[»]
	5AYW	X-ray	3.56	D	20-245	[»]
	5D0O	X-ray	2.90	D	1-245	[»]
	5D0Q	X-ray	3.50	D/H	1-245	[»]
	5EKQ	X-ray	3.39	D	20-245	[»]
	5LJO	electron microscopy	4.90	D	26-243	[»]
ProteinModelPortalⁱ	P0AC02
SMRⁱ	P0AC02
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4260615, 311 interactors 851422, 1 interactor
ComplexPortalⁱ	CPX-1923 Bam complex
DIPⁱ	DIP-51120N
IntActⁱ	P0AC02, 6 interactors
MINTⁱ	P0AC02
STRINGⁱ	316385.ECDH10B_2763

Protein family/group databases

TCDBⁱ	1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

TCDBⁱ

1.B.33.1.3 the outer membrane protein insertion porin (bam complex) (ompip) family

Proteomic databases

EPDⁱ	P0AC02
PaxDbⁱ	P0AC02
PRIDEⁱ	P0AC02

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC75644; AAC75644; b2595 BAA16480; BAA16480; BAA16480
GeneIDⁱ	947086
KEGGⁱ	ecj:JW2577 eco:b2595
PATRICⁱ	fig\|1411691.4.peg.4142

Organism-specific databases

EchoBASEⁱ	EB3974
EcoGeneⁱ	EG14222 bamD

Phylogenomic databases

eggNOGⁱ	ENOG4106SNF Bacteria COG4105 LUCA
HOGENOMⁱ	HOG000260923
InParanoidⁱ	P0AC02
KOⁱ	K05807
PhylomeDBⁱ	P0AC02

Enzyme and pathway databases

BioCycⁱ	EcoCyc:G7352-MONOMER

BioCycⁱ

EcoCyc:G7352-MONOMER

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:P0AC02

PROⁱ

PR:P0AC02

Family and domain databases

CDDⁱ	cd15830 BamD, 1 hit
Gene3Dⁱ	1.25.40.10, 1 hit
HAMAPⁱ	MF_00922 OM_assembly_BamD, 1 hit
InterProⁱ	View protein in InterPro IPR017689 BamD IPR039565 BamD-like IPR011990 TPR-like_helical_dom_sf
PANTHERⁱ	PTHR37423 PTHR37423, 1 hit
Pfamⁱ	View protein in Pfam PF13525 YfiO, 1 hit
SUPFAMⁱ	SSF48452 SSF48452, 1 hit
TIGRFAMsⁱ	TIGR03302 OM_YfiO, 1 hit
PROSITEⁱ	View protein in PROSITE PS51257 PROKAR_LIPOPROTEIN, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	BAMD_ECOLI
Accessionⁱ	P0AC02Primary (citable) accession number: P0AC02 Secondary accession number(s): P77146, Q47344
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 8, 2005
	Last sequence update:	November 8, 2005
	Last modified:	November 7, 2018
	This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Uncharacterized protein families (UPF)
List of uncharacterized protein family (UPF) entries
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P0AC02 (BAMD_ECOLI)

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Outer membrane protein assembly factor BamD

bamD

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Phylogenomic databases

Family and domain databases

Experimental Info

<p>This subsection of the ‘Sequence’ section reports information derived from mass spectrometry experiments done on the entire protein or on biologically active derived peptide(s).<p><a href='/help/mass_spectrometry' target='_top'>More...</a></p>Mass spectrometryi

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

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Functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Mass spectrometryⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ