Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 133 (26 Feb 2020)
Sequence version 1 (19 Jul 2005)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Outer membrane protein assembly factor BamA

Gene

bamA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

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 BamD, the core component of the assembly machinery. 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
(Microbial infection) Acts as a receptor for CdiA-EC93, the contact-dependent growth inhibition (CDI) effector of E.coli strain EC93; antibodies against extracellular epitopes decrease CDI. Its role in CDI is independent of the other Bam complex components (PubMed:18761695). Is not the receptor for CdiA from E.coli strain 536 / UPEC, which does not have the same mode of toxicity as CdiA from strain EC93; the decreased expression of bamA101 in some experiments decreases the level of outer membrane proteins in general (PubMed:23469034, PubMed:23882017). Susceptibility to CdiA-EC93 is dependent on E.coli BamA; replacing BamA with the gene from S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii 3937 renders cells resistant to CdiA-EC93. Cells with BamA from another bacteria no longer form CdiA-EC93-induced aggregates with EC93 cells. A chimera in which E.cloacae extracellular loops 6 and 7 are replaced with loops 6 and 7 from E.coli is susceptible to CdiA-EC93 and to CdiA-CT from strain 536 / UPEC (PubMed:23882017).3 Publications

<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

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
EcoCyc:G6093-MONOMER
ECOL316407:JW0172-MONOMER

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Outer membrane protein assembly factor BamAUniRule annotation
Alternative name(s):
Omp85
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:bamAUniRule annotation
Synonyms:yaeT, yzzN, yzzY
Ordered Locus Names:b0177, JW0172
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiEscherichia coli (strain K12)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri83333 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini21 – 424PeriplasmicCuratedAdd BLAST404
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei425 – 433Beta stranded; Name=Strand 11 Publication9
Topological domaini434 – 435Extracellular; loop 1Curated2
Transmembranei436 – 446Beta stranded; Name=Strand 21 PublicationAdd BLAST11
Topological domaini447 – 454PeriplasmicCurated8
Transmembranei455 – 462Beta stranded; Name=Strand 31 Publication8
Topological domaini463 – 465Extracellular; loop 2Curated3
Transmembranei466 – 475Beta stranded; Name=Strand 41 Publication10
Topological domaini476 – 483PeriplasmicCurated8
Transmembranei484 – 495Beta stranded; Name=Strand 51 PublicationAdd BLAST12
Topological domaini496 – 504Extracellular; loop 3Curated9
Transmembranei505 – 506Beta stranded; Name=Strand 61 Publication2
Topological domaini507 – 522PeriplasmicCuratedAdd BLAST16
Transmembranei523 – 535Beta stranded; Name=Strand 71 PublicationAdd BLAST13
Topological domaini536 – 563Extracellular; loop 42 PublicationsAdd BLAST28
Transmembranei564 – 577Beta stranded; Name=Strand 81 PublicationAdd BLAST14
Topological domaini578 – 590PeriplasmicCuratedAdd BLAST13
Transmembranei591 – 600Beta stranded; Name=Strand 91 Publication10
Topological domaini601 – 608Extracellular; loop 5Curated8
Transmembranei609 – 619Beta stranded; Name=Strand 101 PublicationAdd BLAST11
Topological domaini620 – 628PeriplasmicCurated9
Transmembranei629 – 639Beta stranded; Name=Strand 111 PublicationAdd BLAST11
Topological domaini640 – 708Extracellular; loop 62 PublicationsAdd BLAST69
Transmembranei709 – 718Beta stranded; Name=Strand 121 Publication10
Topological domaini719 – 732PeriplasmicCuratedAdd BLAST14
Transmembranei733 – 745Beta stranded; Name=Strand 131 PublicationAdd BLAST13
Topological domaini746 – 767Extracellular; loop 7CuratedAdd BLAST22
Transmembranei768 – 777Beta stranded; Name=Strand 141 Publication10
Topological domaini778PeriplasmicCurated1
Transmembranei779 – 789Beta stranded; Name=Strand 151 PublicationAdd BLAST11
Topological domaini790 – 803Extracellular; loop 8CuratedAdd BLAST14
Transmembranei804 – 808Beta stranded; Name=Strand 161 Publication5

GO - Cellular componenti

Keywords - Cellular componenti

Cell outer membrane, Membrane

<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 subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Deletion is lethal. Depletion results in the accumulation of incorrectly assembled outer membrane proteins, including TolC, OmpF, OmpC and OmpA (PubMed:15851030, PubMed:16102012). Decreased expression leads to decreased susceptibility to contact-dependent growth inhibition (CDI), and decreased expression of outer membrane proteins (including in this study LamB) as well as up-regulation of periplasmic protease DegP (PubMed:18761695, PubMed:23469034).4 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi181N → A: Lethal, protein does not accumulate. 1 Publication1
Mutagenesisi251K → A: Lethal, protein does not accumulate. 1 Publication1
Mutagenesisi259N → A: Lethal, protein does not accumulate. 1 Publication1
Mutagenesisi351 – 353KIR → PIP: Lethal, wild-type protein levels. 1 Publication3
Mutagenesisi351K → P: Reduces cell growth, wild-type protein levels. 1 Publication1
Mutagenesisi366R → E: Severely impairs cell growth, wild-type protein levels. 1 Publication1
Mutagenesisi373E → K: Lethal, wild-type protein levels. 2 Publications1
Mutagenesisi393G → C: No effect. Lethal; when associated with C-584, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi415 – 419VYKVK → PYKVP: Lethal, wild-type protein levels. 1 Publication5
Mutagenesisi415 – 417VYK → PYP: Lethal, wild-type protein levels. 1 Publication3
Mutagenesisi417 – 419KVK → PVP: Lethal, wild-type protein levels. 1 Publication3
Mutagenesisi429G → P: Lethal, wild-type protein levels. 1 Publication1
Mutagenesisi430I → C: Reduced folding of OmpT; when associated with C-808, traps protein in lateral closed conformation, growth restored by reducing agent. 1 Publication1
Mutagenesisi435E → C: No effect. Lethal; when associated with C-658 or C-665, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi435E → L: Very minor growth defect. Lethal; when associated with L-800. 1 Publication1
Mutagenesisi464D → L: Very minor growth defect. 1 Publication1
Mutagenesisi500D → L: Very minor growth defect. 1 Publication1
Mutagenesisi547R → A: Lethal. 1 Publication1
Mutagenesisi554 – 562EHPSTSDQD → VDYPYDVPDYA: Loop 4 to HA epitope; still susceptible to CdiA-EC93. 1 Publication9
Mutagenesisi556 – 563PSTSDQDN → G: Delta loop 4; slight increase in resistance to CdiA-EC93, forms aggregates with CdiA-EC93 cells. 1 Publication8
Mutagenesisi584G → C: No effect. Lethal; when associated with C-393, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi658S → C: No effect. Lethal; when associated with C-435, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi661R → A: Slow growth on solid and liquid media, less protein accumulates which is more proteinase sensitive. 1 Publication1
Mutagenesisi665S → C: No effect. Lethal; when associated with C-435, probably locks protein in a single conformation that prevents movement, growth restored by strong reducing agent. 1 Publication1
Mutagenesisi673 – 702Missing : Lethal. 1 PublicationAdd BLAST30
Mutagenesisi675 – 701FPHQA…KDLCK → G: Delta loop 6; fully resistant to CdiA-EC93, does not form aggregates with CdiA-EC93 cells. 1 PublicationAdd BLAST27
Mutagenesisi677 – 685HQASNYDPD → VDYPYDVPDYA: Loop 6 to HA epitope; still susceptible to CdiA-EC93. 1 Publication9
Mutagenesisi740D → A: Slow growth on solid and liquid media, less protein accumulates which is more proteinase sensitive. 1 Publication1
Mutagenesisi754 – 755YS → VDYPYDVPDYA: Loop 7 to HA epitope; fully resistant to CdiA-EC93, does not form aggregates with CdiA-EC93 cells. 1 Publication2
Mutagenesisi800E → L: Very minor growth defect. Lethal; when associated with L-435. 1 Publication1
Mutagenesisi808K → C: Reduced folding of OmpT; when associated with C-430, traps protein in lateral closed conformation, growth restored by reducing agent. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 20UniRule annotation1 PublicationAdd BLAST20
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003347021 – 810Outer membrane protein assembly factor BamAAdd BLAST790

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P0A940

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0A940

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P0A940

PRoteomics IDEntifications database

More...
PRIDEi
P0A940

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P0A940

PTM databases

CarbonylDB database of protein carbonylation sites

More...
CarbonylDBi
P0A940

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Part of the Bam complex, which is composed of the outer membrane protein BamA, and four lipoproteins BamB, BamC, BamD and BamE. BamA interacts directly with BamB and the BamCDE subcomplex. 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).

10 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
4259504, 747 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1923 Bam complex

Database of interacting proteins

More...
DIPi
DIP-36019N

Protein interaction database and analysis system

More...
IntActi
P0A940, 14 interactors

STRING: functional protein association networks

More...
STRINGi
511145.b0177

<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

1810
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P0A940

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0A940

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 91POTRA 1PROSITE-ProRule annotation1 PublicationAdd BLAST68
Domaini92 – 172POTRA 2PROSITE-ProRule annotation1 PublicationAdd BLAST81
Domaini175 – 263POTRA 3PROSITE-ProRule annotation1 PublicationAdd BLAST89
Domaini266 – 344POTRA 4PROSITE-ProRule annotation1 PublicationAdd BLAST79
Domaini347 – 421POTRA 5PROSITE-ProRule annotation1 PublicationAdd BLAST75

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Contains 5 N-terminal periplasmic polypeptide transport-associated (POTRA) domains which interact with other subunits of the complex, may recruit substrates from the periplasm into the outer membrane and also act as a chaperone (PubMed:17702946, PubMed:18430136, PubMed:19081063, PubMed:21795783, PubMed:14559180). The C-terminal region forms a discontinuous 16-stranded beta-barrel transmembrane region. The central pore is ellipsoid, and probably closed by extracellular loop 6, perhaps with the aid of other loops (PubMed:24914988, PubMed:24619089).1 Publication6 Publications

<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

Belongs to the BamA family.UniRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane beta strand

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG4105E1Z Bacteria
COG4775 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_007664_1_0_6

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0A940

KEGG Orthology (KO)

More...
KOi
K07277

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0A940

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_01430 OM_assembly_BamA, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000184 Bac_surfAg_D15
IPR010827 BamA/TamA_POTRA
IPR039910 D15-like
IPR023707 OM_assembly_BamA
IPR034746 POTRA

The PANTHER Classification System

More...
PANTHERi
PTHR12815 PTHR12815, 1 hit
PTHR12815:SF23 PTHR12815:SF23, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01103 Bac_surface_Ag, 1 hit
PF07244 POTRA, 4 hits

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF006076 OM_assembly_OMP85, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR03303 OM_YaeT, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51779 POTRA, 5 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P0A940-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAMKKLLIAS LLFSSATVYG AEGFVVKDIH FEGLQRVAVG AALLSMPVRT
60 70 80 90 100
GDTVNDEDIS NTIRALFATG NFEDVRVLRD GDTLLVQVKE RPTIASITFS
110 120 130 140 150
GNKSVKDDML KQNLEASGVR VGESLDRTTI ADIEKGLEDF YYSVGKYSAS
160 170 180 190 200
VKAVVTPLPR NRVDLKLVFQ EGVSAEIQQI NIVGNHAFTT DELISHFQLR
210 220 230 240 250
DEVPWWNVVG DRKYQKQKLA GDLETLRSYY LDRGYARFNI DSTQVSLTPD
260 270 280 290 300
KKGIYVTVNI TEGDQYKLSG VEVSGNLAGH SAEIEQLTKI EPGELYNGTK
310 320 330 340 350
VTKMEDDIKK LLGRYGYAYP RVQSMPEIND ADKTVKLRVN VDAGNRFYVR
360 370 380 390 400
KIRFEGNDTS KDAVLRREMR QMEGAWLGSD LVDQGKERLN RLGFFETVDT
410 420 430 440 450
DTQRVPGSPD QVDVVYKVKE RNTGSFNFGI GYGTESGVSF QAGVQQDNWL
460 470 480 490 500
GTGYAVGING TKNDYQTYAE LSVTNPYFTV DGVSLGGRLF YNDFQADDAD
510 520 530 540 550
LSDYTNKSYG TDVTLGFPIN EYNSLRAGLG YVHNSLSNMQ PQVAMWRYLY
560 570 580 590 600
SMGEHPSTSD QDNSFKTDDF TFNYGWTYNK LDRGYFPTDG SRVNLTGKVT
610 620 630 640 650
IPGSDNEYYK VTLDTATYVP IDDDHKWVVL GRTRWGYGDG LGGKEMPFYE
660 670 680 690 700
NFYAGGSSTV RGFQSNTIGP KAVYFPHQAS NYDPDYDYEC ATQDGAKDLC
710 720 730 740 750
KSDDAVGGNA MAVASLEFIT PTPFISDKYA NSVRTSFFWD MGTVWDTNWD
760 770 780 790 800
SSQYSGYPDY SDPSNIRMSA GIALQWMSPL GPLVFSYAQP FKKYDGDKAE
810
QFQFNIGKTW
Length:810
Mass (Da):90,553
Last modified:July 19, 2005 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDDCE4C6D341664EB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti115E → Q in AAK64508 (Ref. 2) Curated1
Sequence conflicti228S → I in AAK64508 (Ref. 2) Curated1
Sequence conflicti361K → R in AAK64508 (Ref. 2) Curated1
Sequence conflicti632R → C in AAK64508 (Ref. 2) Curated1
Sequence conflicti712A → T in AAK64508 (Ref. 2) Curated1

<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

Molecular mass is 88426 Da. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AF407013 Genomic DNA Translation: AAL01379.1
AY035865 Genomic DNA Translation: AAK64508.1
U70214 Genomic DNA Translation: AAB08606.1
U00096 Genomic DNA Translation: AAC73288.1
AP009048 Genomic DNA Translation: BAA77852.2

Protein sequence database of the Protein Information Resource

More...
PIRi
A64742

NCBI Reference Sequences

More...
RefSeqi
NP_414719.1, NC_000913.3
WP_001240896.1, NZ_STEB01000032.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAC73288; AAC73288; b0177
BAA77852; BAA77852; BAA77852

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
944870

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
ecj:JW0172
eco:b0177

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|1411691.4.peg.2102

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<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

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF407013 Genomic DNA Translation: AAL01379.1
AY035865 Genomic DNA Translation: AAK64508.1
U70214 Genomic DNA Translation: AAB08606.1
U00096 Genomic DNA Translation: AAC73288.1
AP009048 Genomic DNA Translation: BAA77852.2
PIRiA64742
RefSeqiNP_414719.1, NC_000913.3
WP_001240896.1, NZ_STEB01000032.1

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 entryMethodResolution (Å)ChainPositionsPDBsum
2QCZX-ray2.70A/B21-351[»]
2QDFX-ray2.20A21-351[»]
2V9HNMR-A21-184[»]
3EFCX-ray3.30A21-410[»]
3OG5X-ray2.69A/B264-424[»]
3Q6BX-ray1.50A266-420[»]
4C4VX-ray3.00A347-810[»]
B344-810[»]
4N75X-ray2.60A/B427-810[»]
4PK1X-ray3.10A175-424[»]
4XGAX-ray2.15B175-420[»]
5AYWX-ray3.56A22-810[»]
5D0OX-ray2.90A1-810[»]
5D0QX-ray3.50A/F1-810[»]
5EKQX-ray3.39A21-810[»]
5LJOelectron microscopy4.90A24-806[»]
SMRiP0A940
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4259504, 747 interactors
ComplexPortaliCPX-1923 Bam complex
DIPiDIP-36019N
IntActiP0A940, 14 interactors
STRINGi511145.b0177

PTM databases

CarbonylDBiP0A940

2D gel databases

SWISS-2DPAGEiP0A940

Proteomic databases

EPDiP0A940
jPOSTiP0A940
PaxDbiP0A940
PRIDEiP0A940

Genome annotation databases

EnsemblBacteriaiAAC73288; AAC73288; b0177
BAA77852; BAA77852; BAA77852
GeneIDi944870
KEGGiecj:JW0172
eco:b0177
PATRICifig|1411691.4.peg.2102

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...
EchoBASEi
EB2541

Phylogenomic databases

eggNOGiENOG4105E1Z Bacteria
COG4775 LUCA
HOGENOMiCLU_007664_1_0_6
InParanoidiP0A940
KOiK07277
PhylomeDBiP0A940

Enzyme and pathway databases

BioCyciEcoCyc:G6093-MONOMER
ECOL316407:JW0172-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0A940

Protein Ontology

More...
PROi
PR:P0A940

Family and domain databases

HAMAPiMF_01430 OM_assembly_BamA, 1 hit
InterProiView protein in InterPro
IPR000184 Bac_surfAg_D15
IPR010827 BamA/TamA_POTRA
IPR039910 D15-like
IPR023707 OM_assembly_BamA
IPR034746 POTRA
PANTHERiPTHR12815 PTHR12815, 1 hit
PTHR12815:SF23 PTHR12815:SF23, 1 hit
PfamiView protein in Pfam
PF01103 Bac_surface_Ag, 1 hit
PF07244 POTRA, 4 hits
PIRSFiPIRSF006076 OM_assembly_OMP85, 1 hit
TIGRFAMsiTIGR03303 OM_YaeT, 1 hit
PROSITEiView protein in PROSITE
PS51779 POTRA, 5 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiBAMA_ECOLI
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P0A940
Secondary accession number(s): P39170
, P39181, P77465, Q548B8, Q8KR94, Q9R2E3
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: February 26, 2020
This is version 133 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again