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Protein

Macrolide export protein MacA

Gene

macA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Part of the tripartite efflux system MacAB-TolC. MacA stimulates the ATPase activity of MacB by promoting the closed ATP-bound state of MacB, increases the capacity of MacB to bind macrolides such as erythromycin, and provides a physical link between MacB and TolC. When overexpressed, the system confers resistance against macrolides composed of 14- and 15-membered lactones but no or weak resistance against 16-membered ones. In addition, MacA binds tightly rough-core lipopolysaccharide (R-LPS), suggesting that the system could also transport R-LPS or a similar glycolipid.5 Publications

GO - Molecular functioni

  • substrate-specific transmembrane transporter activity Source: EcoCyc

GO - Biological processi

  • drug export Source: EcoCyc
  • response to antibiotic Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Antibiotic resistance, Transport

Enzyme and pathway databases

BioCyciEcoCyc:MACA.
ECOL316407:JW0862-MONOMER.

Protein family/group databases

TCDBi3.A.1.122.1. the atp-binding cassette (abc) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Macrolide export protein MacA
Gene namesi
Name:macA
Synonyms:ybjY
Ordered Locus Names:b0878, JW0862
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13694. macA.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 10CytoplasmicSequence analysis10
Transmembranei11 – 31HelicalSequence analysisAdd BLAST21
Topological domaini32 – 371PeriplasmicSequence analysisAdd BLAST340

GO - Cellular componenti

  • extrinsic component of membrane Source: EcoliWiki
  • integral component of membrane Source: UniProtKB-KW
  • plasma membrane Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi353G → A: 2-fold increase in susceptibility to macrolides. Does not affect oligomerization and ability to interact with MacB and TolC, but changes the structure of the MP region. Does not stimulate MacB ATPase activity. 1 Publication1
Mutagenesisi353G → C: 4-fold increase in susceptibility to macrolides. Does not stimulate MacB ATPase activity. 1 Publication1
Mutagenesisi353G → S: 2-fold increase in susceptibility to macrolides. 1 Publication1
Mutagenesisi357G → A: 2-fold increase in susceptibility to macrolides. Does not stimulate MacB ATPase activity. 1 Publication1
Mutagenesisi357G → C or S: Does not affect susceptibility to macrolides. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000186951 – 371Macrolide export protein MacAAdd BLAST371

Proteomic databases

PaxDbiP75830.
PRIDEiP75830.

Expressioni

Inductioni

Expressed at very low levels under standard laboratory conditions.1 Publication

Interactioni

Subunit structurei

Homohexamer. Part of the tripartite efflux system MacAB-TolC, which is composed of an inner membrane transporter, MacB, a periplasmic membrane fusion protein, MacA, and an outer membrane component, TolC. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes. MacA interacts with MacB and TolC, and this interaction changes its conformation.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-551961,EBI-551961
macBP758312EBI-551961,EBI-1125580

Protein-protein interaction databases

BioGridi4260003. 347 interactors.
DIPiDIP-11460N.
IntActiP75830. 9 interactors.
STRINGi511145.b0878.

Structurei

Secondary structure

1371
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi49 – 63Combined sources15
Beta strandi70 – 75Combined sources6
Beta strandi88 – 92Combined sources5
Helixi95 – 125Combined sources31
Helixi127 – 137Combined sources11
Beta strandi139 – 141Combined sources3
Helixi144 – 155Combined sources12
Helixi157 – 169Combined sources13
Helixi171 – 174Combined sources4
Turni175 – 182Combined sources8
Beta strandi183 – 187Combined sources5
Beta strandi189 – 199Combined sources11
Beta strandi215 – 218Combined sources4
Beta strandi221 – 228Combined sources8
Helixi231 – 233Combined sources3
Beta strandi248 – 253Combined sources6
Beta strandi259 – 262Combined sources4
Beta strandi268 – 271Combined sources4
Beta strandi276 – 282Combined sources7
Beta strandi284 – 286Combined sources3
Beta strandi293 – 300Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FPPX-ray2.99A/B31-371[»]
ProteinModelPortaliP75830.
SMRiP75830.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP75830.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili92 – 137Sequence analysisAdd BLAST46

Domaini

The periplasmic domain is sufficient to bind MacB. The membrane proximal (MP) region plays a critical role in the stimulation of MacB ATPase activity.2 Publications

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105DJY. Bacteria.
COG0845. LUCA.
HOGENOMiHOG000216993.
InParanoidiP75830.
KOiK13888.
OMAiRINPAIN.
PhylomeDBiP75830.

Family and domain databases

InterProiIPR032317. HlyD_D23.
IPR030190. MacA.
IPR006143. RND_pump_MFP.
[Graphical view]
PANTHERiPTHR30572:SF10. PTHR30572:SF10. 1 hit.
PfamiPF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01730. RND_mfp. 1 hit.

Sequencei

Sequence statusi: Complete.

P75830-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRKTVKKR YVIALVIVIA GLITLWRILN APVPTYQTLI VRPGDLQQSV
60 70 80 90 100
LATGKLDALR KVDVGAQVSG QLKTLSVAIG DKVKKDQLLG VIDPEQAENQ
110 120 130 140 150
IKEVEATLME LRAQRQQAEA ELKLARVTYS RQQRLAQTKA VSQQDLDTAA
160 170 180 190 200
TEMAVKQAQI GTIDAQIKRN QASLDTAKTN LDYTRIVAPM AGEVTQITTL
210 220 230 240 250
QGQTVIAAQQ APNILTLADM SAMLVKAQVS EADVIHLKPG QKAWFTVLGD
260 270 280 290 300
PLTRYEGQIK DVLPTPEKVN DAIFYYARFE VPNPNGLLRL DMTAQVHIQL
310 320 330 340 350
TDVKNVLTIP LSALGDPVGD NRYKVKLLRN GETREREVTI GARNDTDVEI
360 370
VKGLEAGDEV VIGEAKPGAA Q
Length:371
Mass (Da):40,624
Last modified:May 30, 2000 - v2
Checksum:i8BF287DA03B92AF9
GO

Sequence cautioni

The sequence BAB64541 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB071145 Genomic DNA. Translation: BAB64541.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73965.2.
AP009048 Genomic DNA. Translation: BAA35597.1.
PIRiF64826.
RefSeqiNP_415399.4. NC_000913.3.
WP_000746442.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73965; AAC73965; b0878.
BAA35597; BAA35597; BAA35597.
GeneIDi947322.
KEGGiecj:JW0862.
eco:b0878.
PATRICi32116965. VBIEscCol129921_0908.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB071145 Genomic DNA. Translation: BAB64541.1. Different initiation.
U00096 Genomic DNA. Translation: AAC73965.2.
AP009048 Genomic DNA. Translation: BAA35597.1.
PIRiF64826.
RefSeqiNP_415399.4. NC_000913.3.
WP_000746442.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FPPX-ray2.99A/B31-371[»]
ProteinModelPortaliP75830.
SMRiP75830.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4260003. 347 interactors.
DIPiDIP-11460N.
IntActiP75830. 9 interactors.
STRINGi511145.b0878.

Protein family/group databases

TCDBi3.A.1.122.1. the atp-binding cassette (abc) superfamily.

Proteomic databases

PaxDbiP75830.
PRIDEiP75830.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73965; AAC73965; b0878.
BAA35597; BAA35597; BAA35597.
GeneIDi947322.
KEGGiecj:JW0862.
eco:b0878.
PATRICi32116965. VBIEscCol129921_0908.

Organism-specific databases

EchoBASEiEB3458.
EcoGeneiEG13694. macA.

Phylogenomic databases

eggNOGiENOG4105DJY. Bacteria.
COG0845. LUCA.
HOGENOMiHOG000216993.
InParanoidiP75830.
KOiK13888.
OMAiRINPAIN.
PhylomeDBiP75830.

Enzyme and pathway databases

BioCyciEcoCyc:MACA.
ECOL316407:JW0862-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP75830.
PROiP75830.

Family and domain databases

InterProiIPR032317. HlyD_D23.
IPR030190. MacA.
IPR006143. RND_pump_MFP.
[Graphical view]
PANTHERiPTHR30572:SF10. PTHR30572:SF10. 1 hit.
PfamiPF16576. HlyD_D23. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01730. RND_mfp. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiMACA_ECOLI
AccessioniPrimary (citable) accession number: P75830
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, 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.