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Q7TXL6 (PPSE_MYCBO) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsE
Alternative name(s):
Beta-ketoacyl-acyl-carrier-protein synthase I
EC=2.3.1.41
Gene names
Name:ppsE
Ordered Locus Names:Mb2960
OrganismMycobacterium bovis (strain ATCC BAA-935 / AF2122/97) [Complete proteome] [HAMAP]
Taxonomic identifier233413 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length1488 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the elongation of either C22-24 fatty acids or p-hydroxyphenylalkanoic acids by the addition of malonyl-CoA and methylmalonyl-CoA extender units to yield phthiocerol and phenolphthiocerol derivatives, respectively. Ref.2

Catalytic activity

Acyl-[acyl-carrier-protein] + malonyl-[acyl-carrier-protein] = 3-oxoacyl- [acyl-carrier-protein] + CO2 + [acyl-carrier-protein].

Cofactor

Binds 1 phosphopantetheines covalently By similarity.

NADP By similarity.

Pathway

Lipid metabolism; fatty acid biosynthesis.

Disruption phenotype

Cells lacking this genes abolish the biosynthesis of phthiocerol/phenolphthiocerol dimycocerosate (DIM) and decreased the efficiency with which bacteria infected macrophages derived from monocytes (MDMs). Ref.2

Sequence similarities

Contains 1 acyl carrier domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14881488Phthiocerol/phenolphthiocerol synthesis polyketide synthase type I PpsE
PRO_0000406951

Regions

Domain935 – 100167Acyl carrier
Nucleotide binding1286 – 133146NADP By similarity
Region6 – 389384Beta-ketoacyl synthase By similarity
Region551 – 868318Acyltransferase By similarity

Sites

Active site1841For beta-ketoacyl synthase activity By similarity
Active site6411For malonyltransferase activity By similarity

Amino acid modifications

Modified residue9651O-(pantetheine 4'-phosphoryl)serine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7TXL6 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 14EC40432DB7F502

FASTA1,488158,746
        10         20         30         40         50         60 
MSIPENAIAV VGMAGRFPGA KDVSAFWSNL RRGKESIVTL SEQELRDAGV SDKTLADPAY 

        70         80         90        100        110        120 
VRRAPLLDGI DEFDAGFFGF PPLAAQVLDP QHRLFLQCAW HALEDAGADP ARFDGSIGVY 

       130        140        150        160        170        180 
GTSSPSGYLL HNLLSHRDPN AVLAEGLNFD QFSLFLQNDK DFLATRISHA FNLRGPSIAV 

       190        200        210        220        230        240 
QTACSSSLVA VHLACLSLLS GECDMALAGG SSLCIPHRVG YFTSPGSMVS AVGHCRPFDV 

       250        260        270        280        290        300 
RADGTVFGSG VGLVVLKPLA AAIDAGDRIH AVIRGSAINN DGSAKMGYAA PNPAAQADVI 

       310        320        330        340        350        360 
AEAHAVSGID SSTVSYVECH GTGTPLGDPI EIQGLRAAFE VSQTSRSAPC VLGSVKSNIG 

       370        380        390        400        410        420 
HLEVAAGIAG LIKTILCLKN KALPATLHYT SPNPELRLDQ SPFVVQSKYG PWECDGVRRA 

       430        440        450        460        470        480 
GVSSFGVGGT NAHVVLEEAP AEASEVSAHA EPAGPQVILL SAQTAAALGE SRTALAAALE 

       490        500        510        520        530        540 
TQDGPRLSDV AYTLARRRKH NVTMAAVVHD REHAATVLRA AEHDNVFVGE AAHDGEHGDR 

       550        560        570        580        590        600 
ADAAPTSDRV VFLFPGQGAQ HVGMAKGLYD TEPVFAQHFD TCAAGFRDET GIDLHAEVFD 

       610        620        630        640        650        660 
GTATDLERID RSQPALFTVE YALAKLVDTF GVRAGAYIGY STGEYIAATL AGVFDLQTAI 

       670        680        690        700        710        720 
KTVSLRARLM HESPPGAMVA VALGPDDVTQ YLPPEVELSA VNDPGNCVVA GPKDQIRALR 

       730        740        750        760        770        780 
QRLTEAGIPV RRVRATHAFH TSAMDPMLGQ FQEFLSRQQL RPPRTPLLSN LTGSWMSDQQ 

       790        800        810        820        830        840 
VVDPASWTRQ ISSPIRFADE LDVVLAAPSR ILVEVGPGGS LTGSAMRHPK WSTTHRTVRL 

       850        860        870        880        890        900 
MRHPLQDVDD RDTFLRALGE LWSAGVEVDW TPRRPAVPHL VSLPGYPFAR QRHWVEPNHT 

       910        920        930        940        950        960 
VWAQAPGANN GSPAGTADGS TAATVDAARN GESQTEVTLQ RIWSQCLGVS SVDRNANFFD 

       970        980        990       1000       1010       1020 
LGGDSLMAIS IAMAAANEGL TITPQDLYEY PTLASLTAAV DASFASSGLA KPPEAQANPA 

      1030       1040       1050       1060       1070       1080 
VPPNVTYFLD RGLRDTGRCR VPLILRLDPK IGLPDIRAVL TAVVNHHDAL RLHLVGNDGI 

      1090       1100       1110       1120       1130       1140 
WEQHIAAPAE FTGLSNRSVP DGVAAGSPEE RAAVLGILAE LLEDQTDPNA PLAAVHIAAA 

      1150       1160       1170       1180       1190       1200 
HGGPHYLCLA IHAMVTDDSS RQILATDIVT AFGQRLAGEE ITLEPVSTGW REWSLRCAAL 

      1210       1220       1230       1240       1250       1260 
ATHPAALDTR SYWIENSTKA TLWLADALPN AHTAHPPRAD ELTKLSSTLS VEQTSELDDG 

      1270       1280       1290       1300       1310       1320 
RRRFRRSIQT ILLAALGRTI AQTVGEGVVA VELEGEGRSV LRPDVDLRRT VGWFTTYYPV 

      1330       1340       1350       1360       1370       1380 
PLACATGLGA LAQLDAVHNT LKSVPHYGIG YGLLRYVYAP TGRVLGAQRT PDIHFRYAGV 

      1390       1400       1410       1420       1430       1440 
IPELPSGDAP VQFDSDMTLP VREPIPGMGH AIELRVYRFG GSLHLDWWYD TRRIPAATAE 

      1450       1460       1470       1480 
ALERTFPLAL SALIQEAIAA EHTEHDDSEI VGEPEAGALV DLSSMDAG 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Mycobacterium bovis."
Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. expand/collapse author list , Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.
Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-935 / AF2122/97.
[2]"Phthiocerol dimycocerosates of M. tuberculosis participate in macrophage invasion by inducing changes in the organization of plasma membrane lipids."
Astarie-Dequeker C., Le Guyader L., Malaga W., Seaphanh F.K., Chalut C., Lopez A., Guilhot C.
PLoS Pathog. 5:E1000289-E1000289(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN THE PHTHIOCEROL AND PHENOLPHTHIOCEROL BIOSYNTHESIS, DISRUPTION PHENOTYPE.
Strain: BCG / Pasteur.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248333 Genomic DNA. Translation: CDO44227.1.
RefSeqNP_856605.1. NC_002945.3.

3D structure databases

ProteinModelPortalQ7TXL6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING233413.Mb2960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD96647; CAD96647; Mb2960.
GeneID1092146.
KEGGmbo:Mb2960.
PATRIC18008232. VBIMycBov88188_3248.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1020.
HOGENOMHOG000046292.
KOK12444.
OMAFDECATA.
OrthoDBEOG6QP0WP.

Enzyme and pathway databases

UniPathwayUPA00094.

Family and domain databases

Gene3D1.10.1200.10. 1 hit.
3.40.366.10. 2 hits.
3.40.47.10. 2 hits.
InterProIPR001227. Ac_transferase_dom.
IPR009081. Acyl_carrier_prot-like.
IPR014043. Acyl_transferase.
IPR016035. Acyl_Trfase/lysoPLipase.
IPR001242. Condensatn.
IPR018201. Ketoacyl_synth_AS.
IPR014031. Ketoacyl_synth_C.
IPR014030. Ketoacyl_synth_N.
IPR016036. Malonyl_transacylase_ACP-bd.
IPR020801. PKS_acyl_transferase.
IPR016039. Thiolase-like.
IPR016038. Thiolase-like_subgr.
[Graphical view]
PfamPF00698. Acyl_transf_1. 1 hit.
PF00668. Condensation. 1 hit.
PF00109. ketoacyl-synt. 1 hit.
PF02801. Ketoacyl-synt_C. 1 hit.
PF00550. PP-binding. 1 hit.
[Graphical view]
SMARTSM00827. PKS_AT. 1 hit.
[Graphical view]
SUPFAMSSF47336. SSF47336. 1 hit.
SSF52151. SSF52151. 2 hits.
SSF53901. SSF53901. 3 hits.
SSF55048. SSF55048. 1 hit.
PROSITEPS50075. ACP_DOMAIN. 1 hit.
PS00606. B_KETOACYL_SYNTHASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPSE_MYCBO
AccessionPrimary (citable) accession number: Q7TXL6
Secondary accession number(s): X2BLX7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2003
Last modified: June 11, 2014
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways