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Protein

Macrolide export ATP-binding/permease protein MacB

Gene

macB

Organism
Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Part of the tripartite efflux system MacAB-TdeA. MacB is a non-canonical ABC transporter that contains transmembrane domains (TMD), which form a pore in the inner membrane, and an ATP-binding domain (NBD), which is responsible for energy generation. Confers resistance against macrolides.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi40 – 47ATPUniRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processAntibiotic resistance, Transport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Macrolide export ATP-binding/permease protein MacBUniRule annotation (EC:3.6.3.-UniRule annotation)
Gene namesi
Name:macB1 PublicationUniRule annotation
OrganismiAggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans)
Taxonomic identifieri714 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeAggregatibacter

Subcellular locationi

  • Cell inner membrane UniRule annotation; Multi-pass membrane protein UniRule annotation

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 268CytoplasmicBy similarityCuratedAdd BLAST268
Transmembranei269 – 289HelicalUniRule annotationAdd BLAST21
Topological domaini290 – 523PeriplasmicBy similarityCuratedAdd BLAST234
Transmembranei524 – 544HelicalUniRule annotationAdd BLAST21
Topological domaini545 – 573CytoplasmicBy similarityCuratedAdd BLAST29
Transmembranei574 – 594HelicalUniRule annotationAdd BLAST21
Topological domaini595 – 607PeriplasmicBy similarityCuratedAdd BLAST13
Transmembranei608 – 628HelicalUniRule annotationAdd BLAST21
Topological domaini629 – 644CytoplasmicBy similarityCuratedAdd BLAST16

GO - Cellular componenti

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutation does not produce a noticeable phenotype or alter the drug resistance profile and the hemolytic activity of A.actinomycetemcomitans.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002699171 – 644Macrolide export ATP-binding/permease protein MacBAdd BLAST644

Proteomic databases

PRIDEiQ2EHL8

Interactioni

Subunit structurei

Homodimer. Part of the tripartite efflux system MacAB-TdeA, which is composed of an inner membrane transporter, MacB, a periplasmic membrane fusion protein, MacA, and an outer membrane component, TdeA. The complex forms a large protein conduit and can translocate molecules across both the inner and outer membranes. Interacts with MacA.1 Publication

Structurei

Secondary structure

1644
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 14Combined sources13
Beta strandi20 – 31Combined sources12
Beta strandi35 – 41Combined sources7
Helixi46 – 53Combined sources8
Beta strandi60 – 66Combined sources7
Beta strandi69 – 71Combined sources3
Helixi76 – 85Combined sources10
Beta strandi87 – 90Combined sources4
Helixi102 – 111Combined sources10
Turni112 – 114Combined sources3
Helixi117 – 130Combined sources14
Helixi134 – 136Combined sources3
Helixi141 – 143Combined sources3
Helixi146 – 157Combined sources12
Turni158 – 161Combined sources4
Beta strandi163 – 169Combined sources7
Turni170 – 173Combined sources4
Helixi176 – 191Combined sources16
Beta strandi195 – 199Combined sources5
Helixi203 – 207Combined sources5
Beta strandi210 – 216Combined sources7
Beta strandi219 – 227Combined sources9
Helixi247 – 263Combined sources17
Turni297 – 299Combined sources3
Beta strandi303 – 314Combined sources12
Helixi319 – 323Combined sources5
Helixi329 – 336Combined sources8
Beta strandi341 – 356Combined sources16
Beta strandi359 – 369Combined sources11
Helixi373 – 377Combined sources5
Beta strandi381 – 384Combined sources4
Helixi389 – 394Combined sources6
Beta strandi398 – 402Combined sources5
Helixi403 – 410Combined sources8
Beta strandi419 – 422Combined sources4
Beta strandi425 – 433Combined sources9
Beta strandi447 – 451Combined sources5
Helixi452 – 458Combined sources7
Beta strandi462 – 464Combined sources3
Beta strandi466 – 472Combined sources7
Beta strandi474 – 476Combined sources3
Helixi478 – 493Combined sources16
Beta strandi498 – 502Combined sources5
Helixi503 – 511Combined sources9
Helixi548 – 556Combined sources9
Helixi561 – 597Combined sources37
Helixi609 – 633Combined sources25
Helixi637 – 641Combined sources5

3D structure databases

ProteinModelPortaliQ2EHL8
SMRiQ2EHL8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ2EHL8

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 242ABC transporterUniRule annotationAdd BLAST239

Sequence similaritiesi

Belongs to the ABC transporter superfamily. Macrolide exporter (TC 3.A.1.122) family. [View classification]UniRule annotation

Keywords - Domaini

Transmembrane, Transmembrane helix

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR003838 ABC_permease_dom
IPR003439 ABC_transporter-like
IPR017871 ABC_transporter_CS
IPR017911 ABC_transptr_macrolide_ATP-bd
IPR025857 MacB_PCD
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00005 ABC_tran, 1 hit
PF02687 FtsX, 1 hit
PF12704 MacB_PCD, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00211 ABC_TRANSPORTER_1, 1 hit
PS50893 ABC_TRANSPORTER_2, 1 hit
PS51267 MACB, 1 hit

Sequencei

Sequence statusi: Complete.

Q2EHL8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNIIEIKQLN RYFGEGENRV HVLKDISLSI ERGDFVAIMG QSGSGKSTLM
60 70 80 90 100
NIIGCLDTAT GGSSKIDGKE TIELTNDQLS DLRSQKFGFI FQRYNLLSSL
110 120 130 140 150
TAAENVALPA IYAGMPQSQR LERAKQLLEK LGLGDKWQNK PNQLSGGQQQ
160 170 180 190 200
RVSIARALMN GGEIILADEP TGALDSHSGE NVMEILRQLH EEGHTIIMVT
210 220 230 240 250
HDKHIAASAN RIIEIKDGEI ISDTQKRQVK SAVKNPSVFK GRFGFSKDQL
260 270 280 290 300
MEAFRMSVSA IVAHKMRSLL TMLGIIIGIT SVVSVVALGN GSQQKILENI
310 320 330 340 350
RGIGTNTMTI FNGNGFGDRR SRHIQNLKIS DANTLSKQSY IQSVTPNTSS
360 370 380 390 400
SGILVVGNKS FTSANLYGIG EQYFDVEGLK LKQGRLLTED DVDQSNQVVV
410 420 430 440 450
LDESAKKAIF ANENPLGKTV IFNKRPFRVI GVVSDQQLGG FPGNSLNLYS
460 470 480 490 500
PYSTVLNKIT GGSRIGSITV KISDDVNSTV AEKSLTELLK SLHGKKDFFI
510 520 530 540 550
MNSDTIKQTI ENTTGTMKLL ISSIAFISLI VGGIGVMNIM LVSVTERTKE
560 570 580 590 600
IGVRMAIGAR QINILQQFLI EAVLICLIGG VAGILLSVLI GVLFNSFITD
610 620 630 640
FSMDFSTASI VTAVLFSTLI GVLFGYMPAK KAAELNPITA LAQE
Length:644
Mass (Da):69,871
Last modified:January 9, 2007 - v2
Checksum:iBA25F3FF3E002234
GO

Sequence cautioni

The sequence ABD38132 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ378165 Genomic DNA Translation: ABD38132.1 Different initiation.

Similar proteinsi

Entry informationi

Entry nameiMACB_AGGAC
AccessioniPrimary (citable) accession number: Q2EHL8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 9, 2007
Last modified: February 28, 2018
This is version 66 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

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