PKSR_BACSU
ID PKSR_BACSU Reviewed; 2543 AA.
AC O31784;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Polyketide synthase PksR;
DE EC=2.3.1.-;
GN Name=pksR; OrderedLocusNames=BSU17220;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP SEQUENCE REVISION TO 731 AND 1926.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [3]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT "A singular enzymatic megacomplex from Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN [4]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. {ECO:0000269|PubMed:17234808}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 3 phosphopantetheines covalently. {ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
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DR EMBL; AL009126; CAB13606.2; -; Genomic_DNA.
DR PIR; F69679; F69679.
DR RefSeq; NP_389604.2; NC_000964.3.
DR RefSeq; WP_003245624.1; NZ_JNCM01000035.1.
DR PDB; 4U3V; X-ray; 1.73 A; A=1124-1395.
DR PDBsum; 4U3V; -.
DR AlphaFoldDB; O31784; -.
DR SMR; O31784; -.
DR STRING; 224308.BSU17220; -.
DR ESTHER; bacsu-PKSR; Thioesterase.
DR PaxDb; O31784; -.
DR PRIDE; O31784; -.
DR EnsemblBacteria; CAB13606; CAB13606; BSU_17220.
DR GeneID; 940036; -.
DR KEGG; bsu:BSU17220; -.
DR PATRIC; fig|224308.179.peg.1867; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG2227; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR InParanoid; O31784; -.
DR OMA; GDWHIAN; -.
DR PhylomeDB; O31784; -.
DR BioCyc; BSUB:BSU17220-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.10.129.110; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 3.
DR Pfam; PF14765; PS-DH; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 3.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR SUPFAM; SSF53901; SSF53901; 2.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acyltransferase; Cytoplasm; Multifunctional enzyme; NADP;
KW Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat;
KW Transferase.
FT CHAIN 1..2543
FT /note="Polyketide synthase PksR"
FT /id="PRO_0000379979"
FT DOMAIN 376..452
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1407..1485
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2134..2208
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 165..269
FT /note="Methyltransferase"
FT REGION 465..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..962
FT /note="Beta-ketoacyl synthase 1"
FT REGION 1531..1949
FT /note="Beta-ketoacyl synthase 2"
FT REGION 2234..2514
FT /note="Thioesterase"
FT ACT_SITE 700
FT /note="For beta-ketoacyl synthase 1 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 1680
FT /note="For beta-ketoacyl synthase 2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 413
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1445
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2168
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT STRAND 1136..1141
FT /evidence="ECO:0007829|PDB:4U3V"
FT HELIX 1145..1148
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1150..1152
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1155..1157
FT /evidence="ECO:0007829|PDB:4U3V"
FT HELIX 1162..1174
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1179..1188
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1199..1207
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1213..1220
FT /evidence="ECO:0007829|PDB:4U3V"
FT TURN 1222..1224
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1227..1237
FT /evidence="ECO:0007829|PDB:4U3V"
FT HELIX 1247..1252
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1254..1256
FT /evidence="ECO:0007829|PDB:4U3V"
FT HELIX 1274..1276
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1279..1285
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1288..1295
FT /evidence="ECO:0007829|PDB:4U3V"
FT HELIX 1310..1324
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1334..1346
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1350..1362
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1365..1373
FT /evidence="ECO:0007829|PDB:4U3V"
FT STRAND 1377..1389
FT /evidence="ECO:0007829|PDB:4U3V"
SQ SEQUENCE 2543 AA; 285109 MW; FE9C74D81EC8CA05 CRC64;
MLNTEDILCK MLFAQLQSIG FFTESKSQPV LENFYGRWFE ESQSILERHQ FLKRTENGHV
PTRSIGTMSE LWKEWNEQKF DLLQDNNMKA MVTLVETALK ALPEILTGKA SATDILFPNS
SMDLVEGVYK NNQVADYFND VLADTLTAYL QERLKQEPEA KIRILEIGAG TGGTSAAVFQ
KLKAWQTHIK EYCYTDLSKA FLMHAENKYG PDNPYLTYKR FNVEEPASEQ HIDAGGYDAV
IAANVLHATK NIRQTLRNAK AVLKKNGLLL LNEISNHNIY SHLTFGLLEG WWLYEDPDLR
IPGCPGLYPD TWKMVLESEG FRYVSFMAEQ SHQLGQQIIA AESNGVVRQK KRTEAEEDPS
HIQMNAEIDH SQESDSLIEQ TAQFVKHTLA KSIKLSPERI HEDTTFEKYG IDSILQVNFI
RELEKVTGEL PKTILFEHNN TKELVEYLVK GHENKLRTAL LKEKTKPAKN EAPLQTERTD
PNKPFTFHTR RFVTEQEVTE TQLANTEPLK IEKTSNLQGT HFNDSSTEDI AIIGVSGRYP
MSNSLEELWG HLIAGDNCIT EAPESRWRTS LLKTLSKDPK KPANKKRYGG FLQDIEAFDH
QLFEVEQNRV MEMTPELRLC LETVWETFED GGYTRTRLDK LRDDDGVGVF IGNMYNQYFW
NIPSLEQAVL SSNGGDWHIA NRVSHFFNLT GPSIAVSSAC SSSLNAIHLA CESLKLKNCS
MAIAGGVNLT LDLSKYDSLE RANLLGSGNQ SKSFGTGNGL IPGEGVGAVL LKPLSKAMED
QDHIYAVIKS SFANHSGGRQ MYTAPDPKQQ AKLIVKSIQQ SGIDPETIGY IESAANGSAL
GDPIEVIALT NAFQQYTNKK QFCAIGSVKS NLGHLEAASG ISQLTKVLLQ MKKGTLVPTI
NAMPVNPNIK LEHTAFYLQE QTEPWHRLND PETGKQLPRR SMINSFGAGG AYANLIIEEY
METAPEKEHI APRQQEFTAV FSAKTKWSLL SYLENMQLFL EKEASLDIEP VVQALHRRNH
NLEHRTAFTV ASTQELIEKL KVFRTSRESS LQQGIYTSFD LQPCAESASR DREINAAEQW
AQGALIAFKE ADIGNRTGWV HLPHYAFDHN TSFHFDVSSI NEKSSDVEDN INQPVIQDQF
TYDEPYVQGH VFNNERVLVG ATYGSLAIEA FFNLFPEENS GRISKLSYIS PIVIKQGETI
ELQAKPLQKD QVIELQIMYR EPSSGLWKPA AIGQCGIGSF EPKKVNIENV KHSLTKLHHI
DQMYKTGNGP EWGELFKTIT HLYRDHKSIL AKIRLPQSGL ANGHHYTVSP LMTNSAYLAI
LSFLEQFDMT GGFLPFGIND IQFTKQTIKG DCWLLITLVK NTGDMLLFDV DVINESSETV
LHYSGYSLKQ LRISNQRGNQ NKAIKASNLK ARIRSYVTDK LAVNMADPSK LSIAKAHIMD
FGIDSSQLVA LTREMEAETK IELNPTLFFE YPTIQELIDF FADKHEASFA QLFGEAHQQE
ERPAQIENQM KQIPAYETNT DKTIEHAADG IAIIGMSGQF PKANSVTEFW DNLVQGKNCV
SEVPKERWDW RKYAAADKEG QSSLQWGGFI EGIGEFDPLF FGISPKEAAN MDPQEFLLLI
HAWKAMEDAG LTGQVLSSRP TGVFVAAGNT DTAVVPSLIP NRISYALDVK GPSEYYEAAC
SSALVALHRA IQSIRNGECE QAIVGAVNLL LSPKGFIGFD SMGYLSEKGQ AKSFQADANG
FVRSEGAGVL IIKPLQKAIE DSDHIYSVIK GSGVSHGGRG MSLHAPNPAG MKDAMLKAYQ
GAQIDPKTVT YIEAHGIASP LADAIEIEAL KSGCSQLELE LPQEVREEAP CYISSLKPSI
GHGELVSGMA ALMKVSMAMK HQTIPGISGF SSLNDQVSLK GTRFRVTAEN QQWRDLSDDA
GKKIPRRASI NSYSFGGVNA HVILEEYIPL PKPPVSMSEN GAHIVVLSAK NQDRLKAIAQ
QQLDYVNKQQ ELSLQDYAYT LQTGREEMED RLALVVRSKE ELVIGLQACL AEKGDKLKSS
VPVFSGNAEN GSSDLEALLD GPLREMVIET LLSENNLEKI AFCWTKGVQI PWEKLYQGKG
ARRIPLPTYP FEKRSCWNGF QAVENTPSVS QDERINNSSD HHILANVLGM APDELQFHKP
LQQYGFDSIS CIQLLQQLQS KVDPLIVLTE LQACHTVQDM MDLIAKKQED TSLQNDQART
FPELIPLNDG KRGRPVFWFH GGVGGVEIYQ QFAQKSQRPF YGIQARGFMT DSAPLHGIEQ
MASYYIEIIR SIQPEGPYDV GGYSLGGMIA YEVTRQLQSQ GLAVKSMVMI DSPYRSETKE
NEASMKTSML QTINTMLASI AKREKFTDVL ISREEVDISL EDEEFLSELI DLAKERGLNK
PDKQIRAQAQ QMMKTQRAYD LESYTVKPLP DPETVKCYYF RNKSRSFFGD LDTYFTLSNE
KEPFDQAAYW EEWERQIPHF HLVDVDSSNH FMILTEPKAS TALLEFCEKL YSNRGVVNAN
FLKAFRKKHE AREEKETDEL VKR
