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Entry version 97 (29 Sep 2021)
Sequence version 1 (09 Jan 2007)
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Protein

Trehalose monomycolate exporter MmpL3

Gene

mmpL3

Organism
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<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

Transports trehalose monomycolate (TMM) to the cell wall (PubMed:31239378, PubMed:22520756, PubMed:28698380).

Flips TMM across the inner membrane. Membrane potential is not required for this function (PubMed:28698380).

Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL) (PubMed:31113875).

Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness (PubMed:28703701).

5 Publications

Miscellaneous

Binds antitubercular compounds N-(4,4-dimethylcyclohexyl)-4,6-difluoro-1H-indole-2-carboxamide (NITD-349) and 1-((2,3-dihydrobenzo[b][1,4]dioxin-6-yl) methyl)-6',7'-dihydrospiro[piperidine-4,4'-thieno[3,2-c]pyran] (SPIRO) with Kd values of 0.05 µM and 0.8 µM, respectively.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by the antimycobacterial compound BM212, a pyrrole derivative (PubMed:28698380). Inhibited by the antitubercular drug SQ109. Inhibited by the adamantyl urea derivative AU1235, the indole carboxamide ICA38 and rimonabant, the antagonist for the cannabinoid receptor CB1. The dissociation constant (Kd) values for SQ109, AU1235, ICA38 and rimonabant are 1.65 µM, 0.29, 0.16 and 29.5, respectively (PubMed:30682372). Inhibitory effects are due to binding of the inhibitors at the proton-transportation channel most likely dissipating the transmembrane electrochemical proton gradient needed for substrate translocation (PubMed:30682372 PubMed:32512002).1 Publication2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei256Part of the proton-transportation channel2 Publications1
Sitei257Part of the proton-transportation channel2 Publications1
Sitei591Part of the proton transportation network1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei645SQ109; inhibitor; antitubercular drugCombined sources1 Publication1
Sitei645Part of the proton-transportation channel3 Publications1
Sitei646Part of the proton-transportation channel2 Publications1
Sitei647Part of the proton transportation network1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processCell wall biogenesis/degradation, Lipid transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MSME246196:G1H7P-260-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Trehalose monomycolate exporter MmpL3Curated
Short name:
TMM exporter MmpL3Curated
Alternative name(s):
MmpL3 transporter1 Publication
Mycobacterial membrane protein large 35 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:mmpL37 PublicationsImported
Ordered Locus Names:MSMEG_0250Imported, MSMEI_0243Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri246196 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycolicibacterium
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000006158 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000757 Componenti: Chromosome

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 14Cytoplasmic2 PublicationsAdd BLAST14
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei15 – 35HelicalSequence analysisAdd BLAST21
Topological domaini36 – 196Periplasmic2 PublicationsAdd BLAST161
Transmembranei197 – 217HelicalSequence analysisAdd BLAST21
Transmembranei218 – 238HelicalSequence analysisAdd BLAST21
Topological domaini239 – 240Periplasmic2 Publications2
Transmembranei241 – 261HelicalSequence analysisAdd BLAST21
Topological domaini262 – 290Cytoplasmic2 PublicationsAdd BLAST29
Transmembranei291 – 311HelicalSequence analysisAdd BLAST21
Topological domaini312 – 317Periplasmic2 Publications6
Transmembranei318 – 338HelicalSequence analysisAdd BLAST21
Topological domaini339 – 401Cytoplasmic2 PublicationsAdd BLAST63
Transmembranei402 – 422HelicalSequence analysisAdd BLAST21
Topological domaini423 – 567Periplasmic2 PublicationsAdd BLAST145
Transmembranei568 – 588HelicalSequence analysisAdd BLAST21
Topological domaini589 – 591Cytoplasmic2 Publications3
Transmembranei592 – 612HelicalSequence analysisAdd BLAST21
Topological domaini613 – 630Periplasmic2 PublicationsAdd BLAST18
Transmembranei631 – 651HelicalSequence analysisAdd BLAST21
Topological domaini652 – 678Cytoplasmic2 PublicationsAdd BLAST27
Transmembranei679 – 699HelicalSequence analysisAdd BLAST21
Topological domaini700 – 703Periplasmic2 Publications4
Transmembranei704 – 724HelicalSequence analysisAdd BLAST21
Topological domaini725 – 1013Cytoplasmic2 PublicationsAdd BLAST289

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

This protein is a target of small molecules which can be validated by developed assays that measure the topology of trehalose monomycolate (TMM) in the inner membrane of mycobacterial spheroplasts after which they may be developed to future antituberculosis drugs (PubMed:28698380). Designing improved inhibitors against this protein could be achieved by avoiding direct contacts with the identified residues that can mutate to confer drug resistance. Alternatively, incorporating conformational flexibility in the inhibitors can allow them to adapt to structural changes in the inhibitor binding pocket due to mutation (PubMed:30682372).2 Publications

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Cells lacking this gene are not viable (PubMed:22520756). Knockdown or depletion of this gene leads to accummulation of trehalose monomycolate (TMM) and lack of trehalose dimycolate (TDM) (PubMed:31239378, PubMed:22520756). Decrease in mycolylation of arabinogalactan (AG) (PubMed:22520756). Accumulates MSMEG_5308 protein (PubMed:31239378).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi40Q → R: Binds to SQ109 with a dissociation constant (Kd) value similar to wild-type. 1 Publication1
Mutagenesisi194I → R: Binds to ICA38 with a dissociation constant (Kd) value similar to wild-type. 1 Publication1
Mutagenesisi301S → A: Binds to SQ109, AU1235, ICA38 and rimonabant with a dissociation constant (Kd) values similar to wild-type; when associated with T-319; L-638 and V-686. 1 Publication1
Mutagenesisi316T → I: Confers resistance to ICA38. 1 Publication1
Mutagenesisi319I → T: Binds to SQ109, AU1235, ICA38 and rimonabant with a dissociation constant (Kd) values similar to wild-type; when associated with A-301; L-638 and V-686. 1 Publication1
Mutagenesisi572I → P: Binds to SQ109 with a dissociation constant (Kd) value similar to wild-type. 1 Publication1
Mutagenesisi596S → I: Confers resistance to ICA38. 1 Publication1
Mutagenesisi638V → L: Binds to SQ109, AU1235, ICA38 and rimonabant with a dissociation constant (Kd) value similar to wild-type; when associated with A-301; T-319 and V-686. 1 Publication1
Mutagenesisi686L → V: Binds to SQ109, AU1235, ICA38 and rimonabant with a dissociation constant (Kd) value similar to wild-type; when associated with A-301; T-319 and L-638. 1 Publication1
Mutagenesisi688V → G: Binds to ICA38 with a dissociation constant (Kd) value similar to wild-type. 1 Publication1
Mutagenesisi689V → G: Binds to ICA38 with a dissociation constant (Kd) value similar to wild-type. 1 Publication1
Mutagenesisi705A → T: Binds to SQ109 with a dissociation constant (Kd) value similar to wild-type. 1 Publication1

<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

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004526861 – 1013Trehalose monomycolate exporter MmpL3Add BLAST1013

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
A0QP27

<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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:30682372, PubMed:31113875).

Interacts with TtfA (via N-terminus); active trehalose monomycolate (TMM) biosynthesis is not required for the complex formation.

Interacts with MSMEG_5308 (PubMed:31239378).

3 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
246196.MSMEI_0243

<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

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
A0QP27

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni40 – 44Phosphatidylethanolamine bindingCombined sources1 Publication5
Regioni485 – 513DisorderedSequence analysisAdd BLAST29
Regioni754 – 1013DisorderedSequence analysisAdd BLAST260

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi492 – 507Basic residues and acidic residuesSequence analysisAdd BLAST16
Compositional biasi754 – 769Basic residues and acidic residuesSequence analysisAdd BLAST16
Compositional biasi778 – 804Pro residuesSequence analysisAdd BLAST27
Compositional biasi978 – 998Basic residues and acidic residuesSequence analysisAdd BLAST21

<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

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
COG2409, Bacteria

Identification of Orthologs from Complete Genome Data

More...
OMAi
SRAYLNW

Database of Orthologous Groups

More...
OrthoDBi
149255at2

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004869, MMPL_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03176, MMPL, 2 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

A0QP27-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFAWWGRTVY QFRYIVIGVM VALCLGGGVY GISLGNHVTQ SGFYDEGSQS
60 70 80 90 100
VAASLIGDEV YGRDRTSHVV AILTPPDDKK VTDKAWQKKV TEELDQVVKD
110 120 130 140 150
HEDQIVGWVG WLKAPDTTDP TVSAMKTQDL RHTFISIPLQ GDDDDEILKN
160 170 180 190 200
YQVVEPELQQ VNGGDIRLAG LNPLASELTG TIGEDQKRAE VAAIPLVAVV
210 220 230 240 250
LFFVFGTVIA AALPAIIGGL AIAGALGIMR LVAEFTPVHF FAQPVVTLIG
260 270 280 290 300
LGIAIDYGLF IVSRFREEIA EGYDTEAAVR RTVMTSGRTV VFSAVIIVAS
310 320 330 340 350
SVPLLLFPQG FLKSITYAII ASVMLAAILS ITVLAAALAI LGPRVDALGV
360 370 380 390 400
TTLLKIPFLA NWQFSRRIID WFAEKTQKTK TREEVERGFW GRLVNVVMKR
410 420 430 440 450
PIAFAAPILV VMVLLIIPLG QLSLGGISEK YLPPDNAVRQ SQEQFDKLFP
460 470 480 490 500
GFRTEPLTLV MKREDGEPIT DAQIADMRAK ALTVSGFTDP DNDPEKMWKE
510 520 530 540 550
RPANDSGSKD PSVRVIQNGL ENRNDAAKKI DELRALQPPH GIEVFVGGTP
560 570 580 590 600
ALEQDSIHSL FDKLPLMALI LIVTTTVLMF LAFGSVVLPI KAALMSALTL
610 620 630 640 650
GSTMGILTWM FVDGHGSGLM NYTPQPLMAP MIGLIIAVIW GLSTDYEVFL
660 670 680 690 700
VSRMVEARER GMSTAEAIRI GTATTGRLIT GAALILAVVA GAFVFSDLVM
710 720 730 740 750
MKYLAFGLLI ALLLDATIIR MFLVPAVMKL LGDDCWWAPR WMKRVQEKLG
760 770 780 790 800
LGETELPDER KRPTVRESET DQRALVGVGA PPPPPRPHDP THPAPEPVRP
810 820 830 840 850
MPPMRSNAPS AAGTARISTP PQPPQPPQAP AQQAGDEPAT TRFAMARNAV
860 870 880 890 900
RNAVNSAVHG GAGSAAAPTE RAPRPGGPAQ PPAPPQREER EIESWLGALR
910 920 930 940 950
GPAPAKNVPQ PPAQPQRPST DTTRAMPPQG RPPAGPADRG NENAPTTAFS
960 970 980 990 1000
AQRPPNGGAP ADATTAIPTP PQREQEPSTE KLNTREDAPE DPETKRRGGG
1010
MSAQDLLRRE GRL
Length:1,013
Mass (Da):109,399
Last modified:January 9, 2007 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i2C0B090D822541E4
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti197V → M Increases resistance to BM212 with 4-fold increase in minimal inhibitory concentration (MIC) to BM212 in liquid and solid media. 1 Publication1
Natural varianti257Y → C Growth defect in both liquid and solid media; confers resistance to SQ109 and AU1235 with 2-fold and 4-fold increased resistance, respectively; disrupted membrane potential; increased cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type. 2 Publications1
Natural varianti293S → A Growth defect in both liquid and solid media; confers resistance to SQ109 and AU1235 with 4-fold and 33-fold increased resistance, respectively; disrupted membrane potential; no significant difference in cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type. 2 Publications1
Natural varianti293S → T Grows as wild-type in liquid media; weak binding to both SQ109 and ICA38 while the dissociation constant (Kd) value for AU1235 increases 6.6-fold compared with wild-type; 8-fold and 4-fold increased resistance to AU1235 and SQ109, respectively; disrupted membrane potential; increased cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type. 2 Publications1
Natural varianti297I → F Growth defect in certain liquid medium; severely reduced binding to SQ109 and AU1235; no change in resistance and 4-fold increased resistance to SQ109 and AU1235, respectively; disrupted membrane potential; increased cell wall hydrophobicity; more sensitive to ampicillin and the hydrophobic antibiotics, rifampicin and erythromycin, but no change in sensitivity to chloramphenicol or kanamycin, compared to wild-type. 2 Publications1
Natural varianti326A → T Increases resistance to BM212 with 4-fold increase in minimal inhibitory concentration (MIC) to BM212 in liquid and solid media. 1 Publication1
Natural varianti750G → D Rescues the growth defect of A-293 variant by partially restoring the membrane potential. 1 Publication1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CP000480 Genomic DNA Translation: ABK74656.1
CP001663 Genomic DNA Translation: AFP36724.1

NCBI Reference Sequences

More...
RefSeqi
WP_011726778.1, NZ_CP009494.1
YP_884665.1, NC_008596.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
ABK74656; ABK74656; MSMEG_0250
AFP36724; AFP36724; MSMEI_0243

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
msg:MSMEI_0243
msm:MSMEG_0250

Pathosystems Resource Integration Center (PATRIC)

More...
PATRICi
fig|246196.19.peg.246

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000480 Genomic DNA Translation: ABK74656.1
CP001663 Genomic DNA Translation: AFP36724.1
RefSeqiWP_011726778.1, NZ_CP009494.1
YP_884665.1, NC_008596.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6AJFX-ray2.70A1-748[»]
6AJGX-ray2.60A1-748[»]
6AJHX-ray2.82A1-748[»]
6AJIX-ray2.90A1-748[»]
6AJJX-ray2.79A1-748[»]
6N40X-ray3.31A1-773[»]
6OR2X-ray2.59A1-773[»]
7C2MX-ray3.10A1-748[»]
7C2NX-ray2.82A1-748[»]
SMRiA0QP27
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi246196.MSMEI_0243

Proteomic databases

PRIDEiA0QP27

Genome annotation databases

EnsemblBacteriaiABK74656; ABK74656; MSMEG_0250
AFP36724; AFP36724; MSMEI_0243
KEGGimsg:MSMEI_0243
msm:MSMEG_0250
PATRICifig|246196.19.peg.246

Phylogenomic databases

eggNOGiCOG2409, Bacteria
OMAiSRAYLNW
OrthoDBi149255at2

Enzyme and pathway databases

BioCyciMSME246196:G1H7P-260-MONOMER

Family and domain databases

InterProiView protein in InterPro
IPR004869, MMPL_dom
PfamiView protein in Pfam
PF03176, MMPL, 2 hits

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMMPL3_MYCS2
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: A0QP27
Secondary accession number(s): I7G2R2
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 2, 2021
Last sequence update: January 9, 2007
Last modified: September 29, 2021
This is version 97 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

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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