UniProtKB - P31224 (ACRB_ECOLI)

BLAST

>sp|P31224|ACRB_ECOLI Multidrug efflux pump subunit AcrB OS=Escherichia coli (strain K12) OX=83333 GN=acrB PE=1 SV=1
MPNFFIDRPIFAWVIAIIIMLAGGLAILKLPVAQYPTIAPPAVTISASYPGADAKTVQDT
VTQVIEQNMNGIDNLMYMSSNSDSTGTVQITLTFESGTDADIAQVQVQNKLQLAMPLLPQ
EVQQQGVSVEKSSSSFLMVVGVINTDGTMTQEDISDYVAANMKDAISRTSGVGDVQLFGS
QYAMRIWMNPNELNKFQLTPVDVITAIKAQNAQVAAGQLGGTPPVKGQQLNASIIAQTRL
TSTEEFGKILLKVNQDGSRVLLRDVAKIELGGENYDIIAEFNGQPASGLGIKLATGANAL
DTAAAIRAELAKMEPFFPSGLKIVYPYDTTPFVKISIHEVVKTLVEAIILVFLVMYLFLQ
NFRATLIPTIAVPVVLLGTFAVLAAFGFSINTLTMFGMVLAIGLLVDDAIVVVENVERVM
AEEGLPPKEATRKSMGQIQGALVGIAMVLSAVFVPMAFFGGSTGAIYRQFSITIVSAMAL
SVLVALILTPALCATMLKPIAKGDHGEGKKGFFGWFNRMFEKSTHHYTDSVGGILRSTGR
YLVLYLIIVVGMAYLFVRLPSSFLPDEDQGVFMTMVQLPAGATQERTQKVLNEVTHYYLT
KEKNNVESVFAVNGFGFAGRGQNTGIAFVSLKDWADRPGEENKVEAITMRATRAFSQIKD
AMVFAFNLPAIVELGTATGFDFELIDQAGLGHEKLTQARNQLLAEAAKHPDMLTSVRPNG
LEDTPQFKIDIDQEKAQALGVSINDINTTLGAAWGGSYVNDFIDRGRVKKVYVMSEAKYR
MLPDDIGDWYVRAADGQMVPFSAFSSSRWEYGSPRLERYNGLPSMEILGQAAPGKSTGEA
MELMEQLASKLPTGVGYDWTGMSYQERLSGNQAPSLYAISLIVVFLCLAALYESWSIPFS
VMLVVPLGVIGALLAATFRGLTNDVYFQVGLLTTIGLSAKNAILIVEFAKDLMDKEGKGL
IEATLDAVRMRLRPILMTSLAFILGVMPLVISTGAGSGAQNAVGTGVMGGMVTATVLAIF
FVPVFFVVVRRRFSRKNEDIEHSHTVDHH

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Format
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History
Entry version 173 (07 Nov 2018)
Sequence version 1 (01 Jul 1993)
Previous versions | rss
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Protein

Multidrug efflux pump subunit AcrB

Gene

acrB

Organism

Escherichia coli (strain K12)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates.4 Publications

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.1 Publication

GO - Molecular functionⁱ

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

drug transmembrane transport
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 8550435
response to drug
Source: EcoCyc
Inferred from mutant phenotypeⁱ
- 8407802

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Transport

Biological process

Transport

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ACRB-MONOMER MetaCyc:ACRB-MONOMER

BioCycⁱ

EcoCyc:ACRB-MONOMER
MetaCyc:ACRB-MONOMER

Protein family/group databases

TCDBⁱ	2.A.6.2.2 the resistance-nodulation-cell division (rnd) superfamily

TCDBⁱ

2.A.6.2.2 the resistance-nodulation-cell division (rnd) superfamily

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Multidrug efflux pump subunit AcrB Alternative name(s): AcrAB-TolC multidrug efflux pump subunit AcrB Acridine resistance protein B
Gene namesⁱ	Name:acrB Synonyms:acrE Ordered Locus Names:b0462, JW0451
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	EG11704 acrB

EcoGeneⁱ

EG11704 acrB

Subcellular locationⁱ

Cell inner membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system."
  Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.
  Mol. Microbiol. 53:697-706(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: INTERACTION WITH ACRA AND TOLC, SUBUNIT, SUBCELLULAR LOCATION.
- Ref.9
  "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.
; Multi-pass membrane protein
2 Publications
Manual assertion based on experiment inⁱ
- Ref.8
  "Interactions underlying assembly of the Escherichia coli AcrAB-TolC multidrug efflux system."
  Touze T., Eswaran J., Bokma E., Koronakis E., Hughes C., Koronakis V.
  Mol. Microbiol. 53:697-706(2004) [PubMed] [Europe PMC] [Abstract]
  Cited for: INTERACTION WITH ACRA AND TOLC, SUBUNIT, SUBCELLULAR LOCATION.
- Ref.9
  "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.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 9	Cytoplasmic1 Publication	9
Transmembraneⁱ	10 – 28	Helical; Name=1Add BLAST	19
Topological domainⁱ	29 – 336	Periplasmic1 PublicationAdd BLAST	308
Transmembraneⁱ	337 – 356	Helical; Name=2Add BLAST	20
Topological domainⁱ	357 – 365	Cytoplasmic1 Publication	9
Transmembraneⁱ	366 – 385	Helical; Name=3Add BLAST	20
Topological domainⁱ	386 – 391	Periplasmic1 Publication	6
Transmembraneⁱ	392 – 413	Helical; Name=4Add BLAST	22
Topological domainⁱ	414 – 438	Cytoplasmic1 PublicationAdd BLAST	25
Transmembraneⁱ	439 – 457	Helical; Name=5Add BLAST	19
Topological domainⁱ	458 – 465	Periplasmic1 Publication	8
Transmembraneⁱ	466 – 490	Helical; Name=6Add BLAST	25
Topological domainⁱ	491 – 538	Cytoplasmic1 PublicationAdd BLAST	48
Transmembraneⁱ	539 – 555	Helical; Name=7Add BLAST	17
Topological domainⁱ	556 – 871	Periplasmic1 PublicationAdd BLAST	316
Transmembraneⁱ	872 – 888	Helical; Name=8Add BLAST	17
Topological domainⁱ	889 – 898	Cytoplasmic1 Publication	10
Transmembraneⁱ	899 – 918	Helical; Name=9Add BLAST	20
Topological domainⁱ	919 – 924	Periplasmic1 Publication	6
Transmembraneⁱ	925 – 943	Helical; Name=10Add BLAST	19
Topological domainⁱ	944 – 972	Cytoplasmic1 PublicationAdd BLAST	29
Transmembraneⁱ	973 – 992	Helical; Name=11Add BLAST	20
Topological domainⁱ	993 – 998	Periplasmic1 Publication	6
Transmembraneⁱ	999 – 1018	Helical; Name=12Add BLAST	20
Topological domainⁱ	1019 – 1049	Cytoplasmic1 PublicationAdd BLAST	31

GO - Cellular componentⁱ

efflux pump complex
Source: EcoCyc
Inferred from physical interactionⁱ
- 15155734
integral component of plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 8407802
membrane
Source: UniProtKB
Inferred from high throughput direct assayⁱ
- 16858726
plasma membrane
Source: EcoCyc
Inferred from direct assayⁱ
- 15919996
- 17309111

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Disruption phenotypeⁱ

Loss of susceptibility to contact-dependent growth inhibition (CDI); inhibiting cells still contact the target.1 Publication

Mutagenesis

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Mutagenesisⁱ	526	H → Y: Partially restores chloramphenicol resistance to an AcrZ G30R mutant. 1 Publication		1

Chemistry databases

ChEMBLⁱ	CHEMBL1681614
Drug and drug target database More...DrugBankⁱ	DB03619 Deoxycholic Acid DB04209 Dequadin DB03825 Rhodamine 6G

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000161811	1 – 1049	Multidrug efflux pump subunit AcrBAdd BLAST		1049

Proteomic databases

EPDⁱ	P31224
PaxDbⁱ	P31224
PRIDEⁱ	P31224

Expressionⁱ

Inductionⁱ

Positively regulated by MarA, Rob and SoxS transcriptional regulators (at protein level).1 Publication

Interactionⁱ

Subunit structureⁱ

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.9 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct
itself		9	EBI-551006,EBI-551006
acrZ	P0AAW9	7	EBI-551006,EBI-6313593
yajC	P0ADZ7	2	EBI-551006,EBI-1130723

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	4259859, 386 interactors
Database of interacting proteins More...DIPⁱ	DIP-9049N
IntActⁱ	P31224, 9 interactors
Molecular INTeraction database More...MINTⁱ	P31224
STRINGⁱ	316385.ECDH10B_0418

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	2 – 6	Combined sources	5
Helixⁱ	9 – 29	Combined sources	21
Beta strandⁱ	32 – 35	Combined sources	4
Beta strandⁱ	42 – 48	Combined sources	7
Helixⁱ	54 – 60	Combined sources	7
Helixⁱ	62 – 66	Combined sources	5
Beta strandⁱ	75 – 83	Combined sources	9
Beta strandⁱ	86 – 94	Combined sources	9
Beta strandⁱ	95 – 97	Combined sources	3
Helixⁱ	100 – 114	Combined sources	15
Helixⁱ	115 – 117	Combined sources	3
Helixⁱ	120 – 123	Combined sources	4
Beta strandⁱ	128 – 130	Combined sources	3
Beta strandⁱ	132 – 144	Combined sources	13
Beta strandⁱ	145 – 147	Combined sources	3
Helixⁱ	151 – 161	Combined sources	11
Helixⁱ	163 – 168	Combined sources	6
Turnⁱ	169 – 171	Combined sources	3
Beta strandⁱ	172 – 179	Combined sources	8
Beta strandⁱ	182 – 188	Combined sources	7
Helixⁱ	190 – 195	Combined sources	6
Helixⁱ	200 – 210	Combined sources	11
Beta strandⁱ	215 – 220	Combined sources	6
Beta strandⁱ	232 – 235	Combined sources	4
Helixⁱ	243 – 247	Combined sources	5
Beta strandⁱ	250 – 253	Combined sources	4
Turnⁱ	255 – 257	Combined sources	3
Beta strandⁱ	259 – 261	Combined sources	3
Helixⁱ	262 – 264	Combined sources	3
Beta strandⁱ	266 – 273	Combined sources	8
Beta strandⁱ	278 – 281	Combined sources	4
Beta strandⁱ	284 – 294	Combined sources	11
Beta strandⁱ	295 – 298	Combined sources	4
Helixⁱ	299 – 313	Combined sources	15
Helixⁱ	314 – 316	Combined sources	3
Beta strandⁱ	317 – 319	Combined sources	3
Beta strandⁱ	321 – 328	Combined sources	8
Helixⁱ	330 – 359	Combined sources	30
Helixⁱ	362 – 385	Combined sources	24
Helixⁱ	392 – 423	Combined sources	32
Helixⁱ	427 – 453	Combined sources	27
Helixⁱ	455 – 458	Combined sources	4
Helixⁱ	461 – 496	Combined sources	36
Turnⁱ	505 – 508	Combined sources	4
Beta strandⁱ	509 – 511	Combined sources	3
Helixⁱ	512 – 536	Combined sources	25
Beta strandⁱ	537 – 539	Combined sources	3
Helixⁱ	540 – 558	Combined sources	19
Beta strandⁱ	561 – 564	Combined sources	4
Beta strandⁱ	571 – 577	Combined sources	7
Helixⁱ	584 – 599	Combined sources	16
Turnⁱ	600 – 605	Combined sources	6
Beta strandⁱ	606 – 616	Combined sources	11
Beta strandⁱ	619 – 631	Combined sources	13
Helixⁱ	634 – 636	Combined sources	3
Helixⁱ	640 – 642	Combined sources	3
Helixⁱ	644 – 655	Combined sources	12
Beta strandⁱ	658 – 660	Combined sources	3
Beta strandⁱ	662 – 666	Combined sources	5
Helixⁱ	672 – 674	Combined sources	3
Beta strandⁱ	679 – 686	Combined sources	8
Helixⁱ	692 – 707	Combined sources	16
Turnⁱ	710 – 712	Combined sources	3
Beta strandⁱ	713 – 720	Combined sources	8
Beta strandⁱ	724 – 731	Combined sources	8
Helixⁱ	733 – 739	Combined sources	7
Helixⁱ	743 – 755	Combined sources	13
Beta strandⁱ	757 – 764	Combined sources	8
Beta strandⁱ	767 – 775	Combined sources	9
Helixⁱ	777 – 779	Combined sources	3
Beta strandⁱ	780 – 782	Combined sources	3
Helixⁱ	783 – 788	Combined sources	6
Beta strandⁱ	790 – 792	Combined sources	3
Beta strandⁱ	794 – 796	Combined sources	3
Beta strandⁱ	798 – 800	Combined sources	3
Helixⁱ	801 – 803	Combined sources	3
Beta strandⁱ	804 – 812	Combined sources	9
Beta strandⁱ	814 – 819	Combined sources	6
Beta strandⁱ	822 – 831	Combined sources	10
Beta strandⁱ	833 – 835	Combined sources	3
Helixⁱ	837 – 848	Combined sources	12
Beta strandⁱ	855 – 859	Combined sources	5
Helixⁱ	861 – 863	Combined sources	3
Beta strandⁱ	865 – 868	Combined sources	4
Turnⁱ	869 – 871	Combined sources	3
Helixⁱ	873 – 892	Combined sources	20
Beta strandⁱ	894 – 897	Combined sources	4
Helixⁱ	898 – 902	Combined sources	5
Helixⁱ	905 – 919	Combined sources	15
Helixⁱ	925 – 954	Combined sources	30
Turnⁱ	955 – 957	Combined sources	3
Helixⁱ	960 – 985	Combined sources	26
Helixⁱ	987 – 990	Combined sources	4
Beta strandⁱ	994 – 996	Combined sources	3
Helixⁱ	997 – 1032	Combined sources	36
Turnⁱ	1033 – 1035	Combined sources	3
Beta strandⁱ	1036 – 1038	Combined sources	3
Beta strandⁱ	1039 – 1041	Combined sources	3

Show more details

3D structure databases

ProteinModelPortalⁱ	P31224
SMRⁱ	P31224
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ

P31224

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the resistance-nodulation-cell division (RND) (TC 2.A.6) family. [View classification]Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105BZS Bacteria COG0841 LUCA
HOGENOMⁱ	HOG000158129
InParanoidⁱ	P31224
KEGG Orthology (KO) More...KOⁱ	K18138
PhylomeDBⁱ	P31224

Family and domain databases

Gene3Dⁱ	3.30.2090.10, 2 hits
InterProⁱ	View protein in InterPro IPR027463 AcrB_DN_DC_subdom IPR001036 Acrflvin-R IPR004764 HAE1
PANTHERⁱ	PTHR32063 PTHR32063, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00873 ACR_tran, 1 hit
PRINTSⁱ	PR00702 ACRIFLAVINRP
SUPFAMⁱ	SSF82714 SSF82714, 2 hits
TIGRFAMsⁱ	TIGR00915 2A0602, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

P31224-1 [UniParc]FASTA Add to basket

« Hide

        10         20         30         40         50
MPNFFIDRPI FAWVIAIIIM LAGGLAILKL PVAQYPTIAP PAVTISASYP 
        60         70         80         90        100
GADAKTVQDT VTQVIEQNMN GIDNLMYMSS NSDSTGTVQI TLTFESGTDA 
       110        120        130        140        150
DIAQVQVQNK LQLAMPLLPQ EVQQQGVSVE KSSSSFLMVV GVINTDGTMT 
       160        170        180        190        200
QEDISDYVAA NMKDAISRTS GVGDVQLFGS QYAMRIWMNP NELNKFQLTP 
       210        220        230        240        250
VDVITAIKAQ NAQVAAGQLG GTPPVKGQQL NASIIAQTRL TSTEEFGKIL 
       260        270        280        290        300
LKVNQDGSRV LLRDVAKIEL GGENYDIIAE FNGQPASGLG IKLATGANAL 
       310        320        330        340        350
DTAAAIRAEL AKMEPFFPSG LKIVYPYDTT PFVKISIHEV VKTLVEAIIL 
       360        370        380        390        400
VFLVMYLFLQ NFRATLIPTI AVPVVLLGTF AVLAAFGFSI NTLTMFGMVL 
       410        420        430        440        450
AIGLLVDDAI VVVENVERVM AEEGLPPKEA TRKSMGQIQG ALVGIAMVLS 
       460        470        480        490        500
AVFVPMAFFG GSTGAIYRQF SITIVSAMAL SVLVALILTP ALCATMLKPI 
       510        520        530        540        550
AKGDHGEGKK GFFGWFNRMF EKSTHHYTDS VGGILRSTGR YLVLYLIIVV 
       560        570        580        590        600
GMAYLFVRLP SSFLPDEDQG VFMTMVQLPA GATQERTQKV LNEVTHYYLT 
       610        620        630        640        650
KEKNNVESVF AVNGFGFAGR GQNTGIAFVS LKDWADRPGE ENKVEAITMR 
       660        670        680        690        700
ATRAFSQIKD AMVFAFNLPA IVELGTATGF DFELIDQAGL GHEKLTQARN 
       710        720        730        740        750
QLLAEAAKHP DMLTSVRPNG LEDTPQFKID IDQEKAQALG VSINDINTTL 
       760        770        780        790        800
GAAWGGSYVN DFIDRGRVKK VYVMSEAKYR MLPDDIGDWY VRAADGQMVP 
       810        820        830        840        850
FSAFSSSRWE YGSPRLERYN GLPSMEILGQ AAPGKSTGEA MELMEQLASK 
       860        870        880        890        900
LPTGVGYDWT GMSYQERLSG NQAPSLYAIS LIVVFLCLAA LYESWSIPFS 
       910        920        930        940        950
VMLVVPLGVI GALLAATFRG LTNDVYFQVG LLTTIGLSAK NAILIVEFAK 
       960        970        980        990       1000
DLMDKEGKGL IEATLDAVRM RLRPILMTSL AFILGVMPLV ISTGAGSGAQ 
      1010       1020       1030       1040 
NAVGTGVMGG MVTATVLAIF FVPVFFVVVR RRFSRKNEDI EHSHTVDHH

Length:1,049

Mass (Da):113,574

Last modified:July 1, 1993 - v1

Checksum:ⁱ19670E3C4CC29055

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M94248 Genomic DNA Translation: AAA23411.1 U00734 Genomic DNA Translation: AAA67135.1 U82664 Genomic DNA Translation: AAB40216.1 U00096 Genomic DNA Translation: AAC73564.1 AP009048 Genomic DNA Translation: BAE76241.1
PIRⁱ	B36938
NCBI Reference Sequences More...RefSeqⁱ	NP_414995.1, NC_000913.3 WP_001132469.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaⁱ	AAC73564; AAC73564; b0462 BAE76241; BAE76241; BAE76241
GeneIDⁱ	945108
KEGGⁱ	ecj:JW0451 eco:b0462
PATRICⁱ	fig\|1411691.4.peg.1814

Protein	Similar proteins		Species	Score	Length	Source
P31224	Multidrug efflux RND transporter permease subunit		Shigella sp.		1049	UniRef100_P31224
Efflux pump membrane transporter		Escherichia coli O145 str. RM9872		1049
Efflux pump membrane transporter		KLEPN		1049
Efflux pump membrane transporter		Escherichia coli D6-113.11		1049
Efflux pump membrane transporter		Escherichia coli M8		1049
+94

Protein	Similar proteins		Species	Score	Length	Source
P31224	Multidrug efflux RND transporter permease subunit		Shigella sp.		1049	UniRef90_P31224
Efflux pump membrane transporter		Escherichia coli O145 str. RM9872		1049
Efflux pump membrane transporter		KLEPN		1049
Efflux pump membrane transporter		Escherichia coli D6-113.11		1049
Efflux pump membrane transporter		Escherichia coli M8		1049
+1539

Protein	Similar proteins		Species	Score	Length	Source
P31224	Multidrug efflux RND transporter permease subunit		Shigella sp.		1049	UniRef50_P31224
Efflux pump membrane transporter		Escherichia coli O145 str. RM9872		1049
Efflux pump membrane transporter		KLEPN		1049
Efflux pump membrane transporter		Escherichia coli D6-113.11		1049
Efflux pump membrane transporter		Escherichia coli M8		1049
+7605

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	M94248 Genomic DNA Translation: AAA23411.1 U00734 Genomic DNA Translation: AAA67135.1 U82664 Genomic DNA Translation: AAB40216.1 U00096 Genomic DNA Translation: AAC73564.1 AP009048 Genomic DNA Translation: BAE76241.1
PIRⁱ	B36938
RefSeqⁱ	NP_414995.1, NC_000913.3 WP_001132469.1, 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
	1IWG	X-ray	3.50	A	1-1049	[»]
	1OY6	X-ray	3.68	A	1-1049	[»]
	1OY8	X-ray	3.63	A	1-1049	[»]
	1OY9	X-ray	3.80	A	1-1049	[»]
	1OYD	X-ray	3.80	A	1-1049	[»]
	1OYE	X-ray	3.48	A	1-1049	[»]
	1T9T	X-ray	3.23	A	1-1049	[»]
	1T9U	X-ray	3.11	A	1-1049	[»]
	1T9V	X-ray	3.80	A	1-1049	[»]
	1T9W	X-ray	3.23	A	1-1049	[»]
	1T9X	X-ray	3.08	A	1-1049	[»]
	1T9Y	X-ray	3.64	A	1-1049	[»]
	2DHH	X-ray	2.80	A/B/C	1-1049	[»]
	2DR6	X-ray	3.30	A/B/C	1-1049	[»]
	2DRD	X-ray	3.10	A/B/C	1-1049	[»]
	2GIF	X-ray	2.90	A/B/C	1-1049	[»]
	2HQC	X-ray	3.56	A	1-1049	[»]
	2HQD	X-ray	3.65	A	1-1049	[»]
	2HQF	X-ray	3.38	A	1-1049	[»]
	2HQG	X-ray	3.38	A	1-1049	[»]
	2HRT	X-ray	3.00	A/B/C/D/E/F	1-1049	[»]
	2I6W	X-ray	3.10	A	1-1049	[»]
	2J8S	X-ray	2.54	A/B/C	1-1049	[»]
	2RDD	X-ray	3.50	A	1-1049	[»]
	2W1B	X-ray	3.85	A	1-1049	[»]
	3AOA	X-ray	3.35	A/B/C	1-1049	[»]
	3AOB	X-ray	3.35	A/B/C	1-1049	[»]
	3AOC	X-ray	3.34	A/B/C	1-1049	[»]
	3AOD	X-ray	3.30	A/B/C	1-1049	[»]
	3D9B	X-ray	3.42	A	1-1049	[»]
	3NOC	X-ray	2.70	A/B/C	1-1049	[»]
	3NOG	X-ray	3.34	A/B/C	1-1049	[»]
	3W9H	X-ray	3.05	A/B/C	1-1033	[»]
	4C48	X-ray	3.30	A	1-1047	[»]
	4CDI	X-ray	3.70	A	1-1049	[»]
	4DX5	X-ray	1.90	A/B/C	1-1049	[»]
	4DX6	X-ray	2.90	A/B/C	1-1049	[»]
	4DX7	X-ray	2.25	A/B/C	1-1049	[»]
	4K7Q	X-ray	3.50	A	1-1049	[»]
	4U8V	X-ray	2.30	A/B/C	1-1049	[»]
	4U8Y	X-ray	2.10	A/B/C	1-1049	[»]
	4U95	X-ray	2.00	A/B/C	1-1049	[»]
	4U96	X-ray	2.20	A/B/C	1-1049	[»]
	4ZIT	X-ray	3.30	A/B/C/D/E/F	1-1049	[»]
	4ZIV	X-ray	3.16	A/B/C/D/E/F	1-1049	[»]
	4ZIW	X-ray	3.40	A/B/C/D/E/F	1-1049	[»]
	4ZJL	X-ray	3.47	A/B/C/D/E/F	1-1049	[»]
	4ZJO	X-ray	3.60	A/B/C/D/E/F	1-1049	[»]
	4ZJQ	X-ray	3.59	A/B/C/D/E/F	1-1049	[»]
	4ZLJ	X-ray	3.26	A	1-1049	[»]
	4ZLL	X-ray	3.36	A	1-1049	[»]
	4ZLN	X-ray	3.56	A	1-1049	[»]
	5EN5	X-ray	2.30	A/B/C	39-329	[»]
				A/B/C	561-869	[»]
	5ENO	X-ray	2.20	A/B/C	39-329	[»]
				A/B/C	561-869	[»]
	5ENP	X-ray	1.90	A/B/C	39-329	[»]
				A/B/C	561-869	[»]
	5ENQ	X-ray	1.80	A/B/C	39-329	[»]
				A/B/C	561-869	[»]
	5ENR	X-ray	2.30	A/B/C	39-329	[»]
				A/B/C	561-869	[»]
	5ENS	X-ray	2.80	A/B/C	39-329	[»]
			A/B/C	561-869	[»]
5ENT	X-ray	2.50	A/B/C	39-329	[»]
			A/B/C	561-869	[»]
5JMN	X-ray	2.50	A/B/C	1-1049	[»]
5NC5	X-ray	3.20	A/B/C	1-1049	[»]
5NG5	electron microscopy	6.50	J/K/L	1-1049	[»]
5O66	electron microscopy	5.90	J/K/L	1-1049	[»]
5V5S	electron microscopy	6.50	J/K/L	1-1049	[»]
5YIL	X-ray	3.00	A/B/C	1-1049	[»]
ProteinModelPortalⁱ	P31224
SMRⁱ	P31224
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	4259859, 386 interactors
DIPⁱ	DIP-9049N
IntActⁱ	P31224, 9 interactors
MINTⁱ	P31224
STRINGⁱ	316385.ECDH10B_0418

Chemistry databases

ChEMBLⁱ	CHEMBL1681614
DrugBankⁱ	DB03619 Deoxycholic Acid DB04209 Dequadin DB03825 Rhodamine 6G

Protein family/group databases

TCDBⁱ	2.A.6.2.2 the resistance-nodulation-cell division (rnd) superfamily

TCDBⁱ

2.A.6.2.2 the resistance-nodulation-cell division (rnd) superfamily

Proteomic databases

EPDⁱ	P31224
PaxDbⁱ	P31224
PRIDEⁱ	P31224

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAC73564; AAC73564; b0462 BAE76241; BAE76241; BAE76241
GeneIDⁱ	945108
KEGGⁱ	ecj:JW0451 eco:b0462
PATRICⁱ	fig\|1411691.4.peg.1814

Organism-specific databases

EchoBASEⁱ	EB1655
EcoGeneⁱ	EG11704 acrB

Phylogenomic databases

eggNOGⁱ	ENOG4105BZS Bacteria COG0841 LUCA
HOGENOMⁱ	HOG000158129
InParanoidⁱ	P31224
KOⁱ	K18138
PhylomeDBⁱ	P31224

Enzyme and pathway databases

BioCycⁱ	EcoCyc:ACRB-MONOMER MetaCyc:ACRB-MONOMER

BioCycⁱ

EcoCyc:ACRB-MONOMER
MetaCyc:ACRB-MONOMER

Miscellaneous databases

EvolutionaryTraceⁱ	P31224
Protein Ontology More...PROⁱ	PR:P31224

Family and domain databases

Gene3Dⁱ	3.30.2090.10, 2 hits
InterProⁱ	View protein in InterPro IPR027463 AcrB_DN_DC_subdom IPR001036 Acrflvin-R IPR004764 HAE1
PANTHERⁱ	PTHR32063 PTHR32063, 1 hit
Pfamⁱ	View protein in Pfam PF00873 ACR_tran, 1 hit
PRINTSⁱ	PR00702 ACRIFLAVINRP
SUPFAMⁱ	SSF82714 SSF82714, 2 hits
TIGRFAMsⁱ	TIGR00915 2A0602, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACRB_ECOLI
Accessionⁱ	P31224Primary (citable) accession number: P31224 Secondary accession number(s): Q2MBW5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
	Last sequence update:	July 1, 1993
	Last modified:	November 7, 2018
	This is version 173 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
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene

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UniProtKB - P31224 (ACRB_ECOLI)

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Multidrug efflux pump subunit AcrB

acrB

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<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

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GO - Biological processi

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Protein family/group databases

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Chemistry databases

<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

Proteomic databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<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

GO - Molecular functioni

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

Miscellaneous 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

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Genome annotation databases

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Protocols and materials databases

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Family and domain databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ