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Protein

Multidrug efflux pump subunit AcrB

Gene

acrB

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  • drug:proton antiporter activity Source: EcoCyc
  • drug transmembrane transporter activity Source: EcoCyc
  • identical protein binding Source: IntAct

GO - Biological processi

  • drug transmembrane transport Source: EcoCyc
  • response to drug Source: EcoCyc
Complete GO annotation...

Keywords - Biological processi

Transport

Enzyme and pathway databases

BioCyciEcoCyc:ACRB-MONOMER.
ECOL316407:JW0451-MONOMER.

Protein family/group databases

TCDBi2.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
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11704. acrB.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 9Cytoplasmic1 Publication9
Transmembranei10 – 28Helical; Name=1Add BLAST19
Topological domaini29 – 336Periplasmic1 PublicationAdd BLAST308
Transmembranei337 – 356Helical; Name=2Add BLAST20
Topological domaini357 – 365Cytoplasmic1 Publication9
Transmembranei366 – 385Helical; Name=3Add BLAST20
Topological domaini386 – 391Periplasmic1 Publication6
Transmembranei392 – 413Helical; Name=4Add BLAST22
Topological domaini414 – 438Cytoplasmic1 PublicationAdd BLAST25
Transmembranei439 – 457Helical; Name=5Add BLAST19
Topological domaini458 – 465Periplasmic1 Publication8
Transmembranei466 – 490Helical; Name=6Add BLAST25
Topological domaini491 – 538Cytoplasmic1 PublicationAdd BLAST48
Transmembranei539 – 555Helical; Name=7Add BLAST17
Topological domaini556 – 871Periplasmic1 PublicationAdd BLAST316
Transmembranei872 – 888Helical; Name=8Add BLAST17
Topological domaini889 – 898Cytoplasmic1 Publication10
Transmembranei899 – 918Helical; Name=9Add BLAST20
Topological domaini919 – 924Periplasmic1 Publication6
Transmembranei925 – 943Helical; Name=10Add BLAST19
Topological domaini944 – 972Cytoplasmic1 PublicationAdd BLAST29
Transmembranei973 – 992Helical; Name=11Add BLAST20
Topological domaini993 – 998Periplasmic1 Publication6
Transmembranei999 – 1018Helical; Name=12Add BLAST20
Topological domaini1019 – 1049Cytoplasmic1 PublicationAdd BLAST31

GO - Cellular componenti

  • integral component of plasma membrane Source: EcoCyc
  • membrane Source: UniProtKB
  • plasma membrane Source: EcoCyc
Complete GO annotation...

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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi526H → Y: Partially restores chloramphenicol resistance to an AcrZ G30R mutant. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1681614.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001618111 – 1049Multidrug efflux pump subunit AcrBAdd BLAST1049

Proteomic databases

EPDiP31224.
PaxDbiP31224.
PRIDEiP31224.

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

WithEntry#Exp.IntActNotes
itself4EBI-551006,EBI-551006
acrZP0AAW94EBI-551006,EBI-6313593

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4259859. 350 interactors.
DIPiDIP-9049N.
IntActiP31224. 8 interactors.
MINTiMINT-1286285.
STRINGi511145.b0462.

Structurei

Secondary structure

11049
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi2 – 6Combined sources5
Helixi9 – 29Combined sources21
Beta strandi32 – 35Combined sources4
Beta strandi42 – 48Combined sources7
Helixi54 – 60Combined sources7
Helixi62 – 66Combined sources5
Beta strandi75 – 83Combined sources9
Beta strandi86 – 94Combined sources9
Beta strandi95 – 97Combined sources3
Helixi100 – 114Combined sources15
Helixi115 – 117Combined sources3
Helixi120 – 123Combined sources4
Beta strandi128 – 130Combined sources3
Beta strandi132 – 144Combined sources13
Beta strandi145 – 147Combined sources3
Helixi151 – 161Combined sources11
Helixi163 – 168Combined sources6
Turni169 – 171Combined sources3
Beta strandi172 – 179Combined sources8
Beta strandi182 – 188Combined sources7
Helixi190 – 195Combined sources6
Helixi200 – 210Combined sources11
Beta strandi215 – 220Combined sources6
Beta strandi232 – 235Combined sources4
Helixi243 – 247Combined sources5
Beta strandi250 – 253Combined sources4
Turni255 – 257Combined sources3
Beta strandi259 – 261Combined sources3
Helixi262 – 264Combined sources3
Beta strandi266 – 273Combined sources8
Beta strandi278 – 281Combined sources4
Beta strandi284 – 294Combined sources11
Beta strandi295 – 298Combined sources4
Helixi299 – 313Combined sources15
Helixi314 – 316Combined sources3
Beta strandi317 – 319Combined sources3
Beta strandi321 – 328Combined sources8
Helixi330 – 359Combined sources30
Helixi362 – 385Combined sources24
Helixi392 – 423Combined sources32
Helixi427 – 453Combined sources27
Helixi455 – 458Combined sources4
Helixi461 – 496Combined sources36
Turni505 – 508Combined sources4
Beta strandi509 – 511Combined sources3
Helixi512 – 536Combined sources25
Beta strandi537 – 539Combined sources3
Helixi540 – 558Combined sources19
Beta strandi561 – 564Combined sources4
Beta strandi571 – 577Combined sources7
Helixi584 – 599Combined sources16
Turni600 – 605Combined sources6
Beta strandi606 – 616Combined sources11
Beta strandi619 – 631Combined sources13
Helixi634 – 636Combined sources3
Helixi640 – 642Combined sources3
Helixi644 – 655Combined sources12
Beta strandi658 – 660Combined sources3
Beta strandi662 – 666Combined sources5
Helixi672 – 674Combined sources3
Beta strandi679 – 686Combined sources8
Helixi692 – 707Combined sources16
Turni710 – 712Combined sources3
Beta strandi713 – 720Combined sources8
Beta strandi724 – 731Combined sources8
Helixi733 – 739Combined sources7
Helixi743 – 755Combined sources13
Beta strandi757 – 764Combined sources8
Beta strandi767 – 775Combined sources9
Helixi777 – 779Combined sources3
Beta strandi780 – 782Combined sources3
Helixi783 – 788Combined sources6
Beta strandi790 – 792Combined sources3
Beta strandi794 – 796Combined sources3
Beta strandi798 – 800Combined sources3
Helixi801 – 803Combined sources3
Beta strandi804 – 812Combined sources9
Beta strandi814 – 819Combined sources6
Beta strandi822 – 831Combined sources10
Beta strandi833 – 835Combined sources3
Helixi837 – 848Combined sources12
Beta strandi855 – 859Combined sources5
Helixi861 – 863Combined sources3
Beta strandi865 – 868Combined sources4
Turni869 – 871Combined sources3
Helixi873 – 892Combined sources20
Beta strandi895 – 897Combined sources3
Helixi898 – 902Combined sources5
Helixi905 – 919Combined sources15
Helixi925 – 954Combined sources30
Turni955 – 957Combined sources3
Helixi960 – 985Combined sources26
Helixi987 – 990Combined sources4
Beta strandi994 – 996Combined sources3
Helixi997 – 1032Combined sources36
Turni1033 – 1035Combined sources3
Beta strandi1036 – 1038Combined sources3
Beta strandi1039 – 1041Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IWGX-ray3.50A1-1049[»]
1OY6X-ray3.68A1-1049[»]
1OY8X-ray3.63A1-1049[»]
1OY9X-ray3.80A1-1049[»]
1OYDX-ray3.80A1-1049[»]
1OYEX-ray3.48A1-1049[»]
1T9TX-ray3.23A1-1049[»]
1T9UX-ray3.11A1-1049[»]
1T9VX-ray3.80A1-1049[»]
1T9WX-ray3.23A1-1049[»]
1T9XX-ray3.08A1-1049[»]
1T9YX-ray3.64A1-1049[»]
2DHHX-ray2.80A/B/C1-1049[»]
2DR6X-ray3.30A/B/C1-1049[»]
2DRDX-ray3.10A/B/C1-1049[»]
2GIFX-ray2.90A/B/C1-1049[»]
2HQCX-ray3.56A1-1049[»]
2HQDX-ray3.65A1-1049[»]
2HQFX-ray3.38A1-1049[»]
2HQGX-ray3.38A1-1049[»]
2HRTX-ray3.00A/B/C/D/E/F1-1049[»]
2I6WX-ray3.10A1-1049[»]
2J8SX-ray2.54A/B/C1-1049[»]
2RDDX-ray3.50A1-1036[»]
2W1BX-ray3.85A1-1049[»]
3AOAX-ray3.35A/B/C1-1049[»]
3AOBX-ray3.35A/B/C1-1049[»]
3AOCX-ray3.34A/B/C1-1049[»]
3AODX-ray3.30A/B/C1-1049[»]
3D9BX-ray3.42A1-1049[»]
3NOCX-ray2.70A/B/C1-1049[»]
3NOGX-ray3.34A/B/C1-1049[»]
3W9HX-ray3.05A/B/C1-1033[»]
4C48X-ray3.30A1-1047[»]
4CDIX-ray3.70A1-1049[»]
4DX5X-ray1.90A/B/C1-1049[»]
4DX6X-ray2.90A/B/C1-1049[»]
4DX7X-ray2.25A/B/C1-1049[»]
4K7QX-ray3.50A1-1049[»]
4U8VX-ray2.30A/B/C1-1049[»]
4U8YX-ray2.10A/B/C1-1049[»]
4U95X-ray2.00A/B/C1-1049[»]
4U96X-ray2.20A/B/C1-1049[»]
4ZITX-ray3.30A/B/C/D/E/F1-1049[»]
4ZIVX-ray3.16A/B/C/D/E/F1-1049[»]
4ZIWX-ray3.40A/B/C/D/E/F1-1049[»]
4ZJLX-ray3.47A/B/C/D/E/F1-1049[»]
4ZJOX-ray3.60A/B/C/D/E/F1-1049[»]
4ZJQX-ray3.59A/B/C/D/E/F1-1049[»]
4ZLJX-ray3.26A1-1049[»]
4ZLLX-ray3.36A1-1049[»]
4ZLNX-ray3.56A1-1049[»]
5EN5X-ray2.30A/B/C39-329[»]
A/B/C561-869[»]
5ENOX-ray2.20A/B/C39-329[»]
A/B/C561-869[»]
5ENPX-ray1.90A/B/C39-329[»]
A/B/C561-869[»]
5ENQX-ray1.80A/B/C39-329[»]
A/B/C561-869[»]
5ENRX-ray2.30A/B/C39-329[»]
A/B/C561-869[»]
5ENSX-ray2.80A/B/C39-329[»]
A/B/C561-869[»]
5ENTX-ray2.50A/B/C39-329[»]
A/B/C561-869[»]
ProteinModelPortaliP31224.
SMRiP31224.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31224.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105BZS. Bacteria.
COG0841. LUCA.
HOGENOMiHOG000158129.
InParanoidiP31224.
KOiK18138.
OMAiKNFLMVI.
PhylomeDBiP31224.

Family and domain databases

Gene3Di3.30.2090.10. 2 hits.
InterProiIPR027463. AcrB_DN_DC_subdom.
IPR001036. Acrflvin-R.
IPR004764. HAE1.
[Graphical view]
PfamiPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSiPR00702. ACRIFLAVINRP.
SUPFAMiSSF82714. SSF82714. 2 hits.
TIGRFAMsiTIGR00915. 2A0602. 1 hit.

Sequencei

Sequence statusi: Complete.

P31224-1 [UniParc]FASTAAdd 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
GO

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.
PIRiB36938.
RefSeqiNP_414995.1. NC_000913.3.
WP_001132469.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73564; AAC73564; b0462.
BAE76241; BAE76241; BAE76241.
GeneIDi945108.
KEGGiecj:JW0451.
eco:b0462.
PATRICi32116077. VBIEscCol129921_0480.

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.
PIRiB36938.
RefSeqiNP_414995.1. NC_000913.3.
WP_001132469.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IWGX-ray3.50A1-1049[»]
1OY6X-ray3.68A1-1049[»]
1OY8X-ray3.63A1-1049[»]
1OY9X-ray3.80A1-1049[»]
1OYDX-ray3.80A1-1049[»]
1OYEX-ray3.48A1-1049[»]
1T9TX-ray3.23A1-1049[»]
1T9UX-ray3.11A1-1049[»]
1T9VX-ray3.80A1-1049[»]
1T9WX-ray3.23A1-1049[»]
1T9XX-ray3.08A1-1049[»]
1T9YX-ray3.64A1-1049[»]
2DHHX-ray2.80A/B/C1-1049[»]
2DR6X-ray3.30A/B/C1-1049[»]
2DRDX-ray3.10A/B/C1-1049[»]
2GIFX-ray2.90A/B/C1-1049[»]
2HQCX-ray3.56A1-1049[»]
2HQDX-ray3.65A1-1049[»]
2HQFX-ray3.38A1-1049[»]
2HQGX-ray3.38A1-1049[»]
2HRTX-ray3.00A/B/C/D/E/F1-1049[»]
2I6WX-ray3.10A1-1049[»]
2J8SX-ray2.54A/B/C1-1049[»]
2RDDX-ray3.50A1-1036[»]
2W1BX-ray3.85A1-1049[»]
3AOAX-ray3.35A/B/C1-1049[»]
3AOBX-ray3.35A/B/C1-1049[»]
3AOCX-ray3.34A/B/C1-1049[»]
3AODX-ray3.30A/B/C1-1049[»]
3D9BX-ray3.42A1-1049[»]
3NOCX-ray2.70A/B/C1-1049[»]
3NOGX-ray3.34A/B/C1-1049[»]
3W9HX-ray3.05A/B/C1-1033[»]
4C48X-ray3.30A1-1047[»]
4CDIX-ray3.70A1-1049[»]
4DX5X-ray1.90A/B/C1-1049[»]
4DX6X-ray2.90A/B/C1-1049[»]
4DX7X-ray2.25A/B/C1-1049[»]
4K7QX-ray3.50A1-1049[»]
4U8VX-ray2.30A/B/C1-1049[»]
4U8YX-ray2.10A/B/C1-1049[»]
4U95X-ray2.00A/B/C1-1049[»]
4U96X-ray2.20A/B/C1-1049[»]
4ZITX-ray3.30A/B/C/D/E/F1-1049[»]
4ZIVX-ray3.16A/B/C/D/E/F1-1049[»]
4ZIWX-ray3.40A/B/C/D/E/F1-1049[»]
4ZJLX-ray3.47A/B/C/D/E/F1-1049[»]
4ZJOX-ray3.60A/B/C/D/E/F1-1049[»]
4ZJQX-ray3.59A/B/C/D/E/F1-1049[»]
4ZLJX-ray3.26A1-1049[»]
4ZLLX-ray3.36A1-1049[»]
4ZLNX-ray3.56A1-1049[»]
5EN5X-ray2.30A/B/C39-329[»]
A/B/C561-869[»]
5ENOX-ray2.20A/B/C39-329[»]
A/B/C561-869[»]
5ENPX-ray1.90A/B/C39-329[»]
A/B/C561-869[»]
5ENQX-ray1.80A/B/C39-329[»]
A/B/C561-869[»]
5ENRX-ray2.30A/B/C39-329[»]
A/B/C561-869[»]
5ENSX-ray2.80A/B/C39-329[»]
A/B/C561-869[»]
5ENTX-ray2.50A/B/C39-329[»]
A/B/C561-869[»]
ProteinModelPortaliP31224.
SMRiP31224.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4259859. 350 interactors.
DIPiDIP-9049N.
IntActiP31224. 8 interactors.
MINTiMINT-1286285.
STRINGi511145.b0462.

Chemistry databases

ChEMBLiCHEMBL1681614.

Protein family/group databases

TCDBi2.A.6.2.2. the resistance-nodulation-cell division (rnd) superfamily.

Proteomic databases

EPDiP31224.
PaxDbiP31224.
PRIDEiP31224.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73564; AAC73564; b0462.
BAE76241; BAE76241; BAE76241.
GeneIDi945108.
KEGGiecj:JW0451.
eco:b0462.
PATRICi32116077. VBIEscCol129921_0480.

Organism-specific databases

EchoBASEiEB1655.
EcoGeneiEG11704. acrB.

Phylogenomic databases

eggNOGiENOG4105BZS. Bacteria.
COG0841. LUCA.
HOGENOMiHOG000158129.
InParanoidiP31224.
KOiK18138.
OMAiKNFLMVI.
PhylomeDBiP31224.

Enzyme and pathway databases

BioCyciEcoCyc:ACRB-MONOMER.
ECOL316407:JW0451-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP31224.
PROiP31224.

Family and domain databases

Gene3Di3.30.2090.10. 2 hits.
InterProiIPR027463. AcrB_DN_DC_subdom.
IPR001036. Acrflvin-R.
IPR004764. HAE1.
[Graphical view]
PfamiPF00873. ACR_tran. 1 hit.
[Graphical view]
PRINTSiPR00702. ACRIFLAVINRP.
SUPFAMiSSF82714. SSF82714. 2 hits.
TIGRFAMsiTIGR00915. 2A0602. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiACRB_ECOLI
AccessioniPrimary (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 30, 2016
This is version 160 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.