ID   PKS15_MYCTU             Reviewed;         496 AA.
AC   P96284; L0TBC2;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 2.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=Putative inactive phenolphthiocerol synthesis polyketide synthase type I Pks15;
GN   Name=pks15; OrderedLocusNames=Rv2947c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   NATURAL FRAMESHIFT.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=12138124; DOI=10.1074/jbc.m206538200;
RA   Constant P., Perez E., Malaga W., Laneelle M.A., Saurel O., Daffe M.,
RA   Guilhot C.;
RT   "Role of the pks15/1 gene in the biosynthesis of phenolglycolipids in the
RT   Mycobacterium tuberculosis complex. Evidence that all strains synthesize
RT   glycosylated p-hydroxybenzoic methyl esters and that strains devoid of
RT   phenolglycolipids harbor a frameshift mutation in the pks15/1 gene.";
RL   J. Biol. Chem. 277:38148-38158(2002).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- CAUTION: M.bovis (strains ATCC BAA-935 / AF2122/97 and BCG / Pasteur
CC       1173P2) and M.marinum (strain ATCC BAA-535 / M) have a single fused
CC       pks15/1 ORF, but M.tuberculosis (strains ATCC 25618 / H37Rv and CDC
CC       1551 / Oshkosh) have 2 separate ORFs. This is due to the natural
CC       deletion of a single base, a guanine, that causes a frameshift and thus
CC       the two ORFs, pks15 and pks1, instead of pks15/1. This frameshift led
CC       to the inactivation of Pks15/1, which in turn caused the inability of
CC       these strains to elongate the putative p-hydroxybenzoic acid precursor
CC       and thus to produce phenolphthiocerol derivatives. {ECO:0000305}.
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DR   EMBL; AL123456; CCP45751.1; -; Genomic_DNA.
DR   PIR; H70668; H70668.
DR   RefSeq; NP_217463.1; NC_000962.3.
DR   RefSeq; WP_009936729.1; NC_000962.3.
DR   AlphaFoldDB; P96284; -.
DR   SMR; P96284; -.
DR   STRING; 83332.Rv2947c; -.
DR   PaxDb; P96284; -.
DR   DNASU; 887291; -.
DR   GeneID; 887291; -.
DR   KEGG; mtu:Rv2947c; -.
DR   TubercuList; Rv2947c; -.
DR   eggNOG; COG3321; Bacteria.
DR   InParanoid; P96284; -.
DR   OMA; MLNDKDF; -.
DR   PhylomeDB; P96284; -.
DR   BRENDA; 2.3.1.261; 3445.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
DR   Gene3D; 3.40.47.10; -; 1.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR036299; Polyketide_synth_docking_sf.
DR   InterPro; IPR016039; Thiolase-like.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SUPFAM; SSF101173; SSF101173; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
DR   PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
PE   1: Evidence at protein level;
KW   Reference proteome.
FT   CHAIN           1..496
FT                   /note="Putative inactive phenolphthiocerol synthesis
FT                   polyketide synthase type I Pks15"
FT                   /id="PRO_0000406363"
FT   REGION          42..471
FT                   /note="Beta-ketoacyl synthase"
FT                   /evidence="ECO:0000250"
FT   REGION          474..496
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   496 AA;  51702 MW;  9842D1A2AF83C643 CRC64;
     MIEEQRTMSV EGADQQSEKL FHYLKKVAVE LDETRARLRE YEQRATEPVA VVGIGCRFPG
     GVDGPDGLWD VVSAGRDVVS EFPTDRGWDV EGLYDPDPDA EGKTYTRWGA FLDDATGFDA
     GFFGIAPSEV LAMDPQQRLM LEVSWEALEH AGIDPLSLRG SATGVYTGIF AASYGNRDTG
     GLQGYGLTGT SISVASGRVS YVLGLQGPAV SVDTACSSSL VAIHWAMSSL RSGECDLALA
     GGVTVMGLPS IFVGFSRQRG LAADGRCKAF AAAADGTGWG EGAGVVVLER LSDARRLGHS
     VLAVVRGSAV NQDGASNGLT APNGLAQQRV IQVALANAGL SAADVDVVEA HGTATTLGDP
     IEAQALLSTY GQGGPAEQPL WVGSIKSNMG HTQAAAGVAG VIKMVQAMRH GVMPATLHVD
     EPSPRVDWTS GAVSVLTEAR EWSVDGRPRR AAVSSFGISG TNAHLILEEA PVPAPAEAPV
     EASESTGGRG RRWCRG