P31224 · ACRB_ECOLI
- ProteinMultidrug efflux pump subunit AcrB
- GeneacrB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1049 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates.
(Microbial infection) Involved in contact-dependent growth inhibition (CDI), acts downstream of BamA, the receptor for CDI. Its role in CDI is independent of the AcrA-AcrB-TolC efflux pump complex.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | efflux pump complex | |
Cellular Component | membrane | |
Cellular Component | periplasmic side of plasma membrane | |
Cellular Component | plasma membrane | |
Molecular Function | alkane transmembrane transporter activity | |
Molecular Function | bile acid transmembrane transporter activity | |
Molecular Function | efflux transmembrane transporter activity | |
Molecular Function | enterobactin transmembrane transporter activity | |
Molecular Function | identical protein binding | |
Molecular Function | xenobiotic transmembrane transporter activity | |
Biological Process | alkane transport | |
Biological Process | bile acid and bile salt transport | |
Biological Process | enterobactin transport | |
Biological Process | fatty acid transport | |
Biological Process | response to antibiotic | |
Biological Process | response to toxic substance | |
Biological Process | response to xenobiotic stimulus | |
Biological Process | xenobiotic detoxification by transmembrane export across the cell outer membrane | |
Biological Process | xenobiotic transport |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMultidrug efflux pump subunit AcrB
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP31224
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-9 | Cytoplasmic | ||||
Sequence: MPNFFIDRP | ||||||
Transmembrane | 10-28 | Helical; Name=1 | ||||
Sequence: IFAWVIAIIIMLAGGLAIL | ||||||
Topological domain | 29-336 | Periplasmic | ||||
Sequence: KLPVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGSQYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRLTSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKIS | ||||||
Transmembrane | 337-356 | Helical; Name=2 | ||||
Sequence: IHEVVKTLVEAIILVFLVMY | ||||||
Topological domain | 357-365 | Cytoplasmic | ||||
Sequence: LFLQNFRAT | ||||||
Transmembrane | 366-385 | Helical; Name=3 | ||||
Sequence: LIPTIAVPVVLLGTFAVLAA | ||||||
Topological domain | 386-391 | Periplasmic | ||||
Sequence: FGFSIN | ||||||
Transmembrane | 392-413 | Helical; Name=4 | ||||
Sequence: TLTMFGMVLAIGLLVDDAIVVV | ||||||
Topological domain | 414-438 | Cytoplasmic | ||||
Sequence: ENVERVMAEEGLPPKEATRKSMGQI | ||||||
Transmembrane | 439-457 | Helical; Name=5 | ||||
Sequence: QGALVGIAMVLSAVFVPMA | ||||||
Topological domain | 458-465 | Periplasmic | ||||
Sequence: FFGGSTGA | ||||||
Transmembrane | 466-490 | Helical; Name=6 | ||||
Sequence: IYRQFSITIVSAMALSVLVALILTP | ||||||
Topological domain | 491-538 | Cytoplasmic | ||||
Sequence: ALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRST | ||||||
Transmembrane | 539-555 | Helical; Name=7 | ||||
Sequence: GRYLVLYLIIVVGMAYL | ||||||
Topological domain | 556-871 | Periplasmic | ||||
Sequence: FVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNGLEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYRMLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEAMELMEQLASKLPTGVGYDWTGMSYQERLSGN | ||||||
Transmembrane | 872-888 | Helical; Name=8 | ||||
Sequence: QAPSLYAISLIVVFLCL | ||||||
Topological domain | 889-898 | Cytoplasmic | ||||
Sequence: AALYESWSIP | ||||||
Transmembrane | 899-918 | Helical; Name=9 | ||||
Sequence: FSVMLVVPLGVIGALLAATF | ||||||
Topological domain | 919-924 | Periplasmic | ||||
Sequence: RGLTND | ||||||
Transmembrane | 925-943 | Helical; Name=10 | ||||
Sequence: VYFQVGLLTTIGLSAKNAI | ||||||
Topological domain | 944-972 | Cytoplasmic | ||||
Sequence: LIVEFAKDLMDKEGKGLIEATLDAVRMRL | ||||||
Transmembrane | 973-992 | Helical; Name=11 | ||||
Sequence: RPILMTSLAFILGVMPLVIS | ||||||
Topological domain | 993-998 | Periplasmic | ||||
Sequence: TGAGSG | ||||||
Transmembrane | 999-1018 | Helical; Name=12 | ||||
Sequence: AQNAVGTGVMGGMVTATVLA | ||||||
Topological domain | 1019-1049 | Cytoplasmic | ||||
Sequence: IFFVPVFFVVVRRRFSRKNEDIEHSHTVDHH |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Loss of susceptibility to contact-dependent growth inhibition (CDI); inhibiting cells still contact the target.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 526 | Partially restores chloramphenicol resistance to an AcrZG30R mutant. | ||||
Sequence: H → Y |
Chemistry
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000161811 | 1-1049 | Multidrug efflux pump subunit AcrB | |||
Sequence: MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDTVTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQEVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGSQYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRLTSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANALDTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQNFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVMAEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMALSVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGRYLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLTKEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKDAMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNGLEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYRMLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEAMELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFSVMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGLIEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIFFVPVFFVVVRRRFSRKNEDIEHSHTVDHH |
Proteomic databases
Expression
Induction
Positively regulated by MarA, Rob and SoxS transcriptional regulators (at protein level).
Interaction
Subunit
Homotrimer, with large domains that extend into the periplasm, interacts with AcrA and TolC. AcrA may be required to stably link this protein and TolC. Interacts with AcrZ. Part of the AcrA-AcrB-AcrZ-TolC efflux pump.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P31224 | acrB P31224 | 9 | EBI-551006, EBI-551006 | |
BINARY | P31224 | acrZ P0AAW9 | 7 | EBI-551006, EBI-6313593 | |
BINARY | P31224 | yajC P0ADZ7 | 2 | EBI-551006, EBI-1130723 |
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length1,049
- Mass (Da)113,574
- Last updated1993-07-01 v1
- Checksum19670E3C4CC29055
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M94248 EMBL· GenBank· DDBJ | AAA23411.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00734 EMBL· GenBank· DDBJ | AAA67135.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U82664 EMBL· GenBank· DDBJ | AAB40216.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC73564.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE76241.1 EMBL· GenBank· DDBJ | Genomic DNA |